Raves ML

General

Full name : Raves Mia L

First name : Mia L

Mail : Dept of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht

Zip Code :

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Country : The Netherlands

Email : mia@nmr.chem.ruu.nl

Phone : 31-30-253-364

Fax : 31-30-253-7623

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References (16)

Title : Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation - Weik_2002_J.Synchrotron.Radiat_9_342
Author(s) : Weik M , Berges J , Raves ML , Gros P , McSweeney S , Silman I , Sussman JL , Houee-Levin C , Ravelli RB
Ref : J Synchrotron Radiat , 9 :342 , 2002
Abstract : Irradiation of proteins with intense X-ray radiation produced by third-generation synchrotron sources generates specific structural and chemical alterations, including breakage of disulfide bonds and decarboxylation. In this paper, disulfide bond lengths in irradiated crystals of the enzyme Torpedo californica acetylcholinesterase are examined based on quantum simulations and on experimental data published previously. The experimental data suggest that one disulfide bond elongates by approximately 0.7 A upon X-ray irradiation as seen in a series of nine data sets collected on a single crystal. Simulation of the same bond suggests elongation by a similar value if a disulfide-radical anion is formed by trapping an electron. The absorption spectrum of a crystal irradiated under similar conditions shows a peak at approximately 400 nm, which in aqueous solution has been attributed to disulfide radicals. The results suggest that the formation of disulfide radicals in protein crystals owing to X-ray irradiation can be observed experimentally, both by structural means and by absorption spectroscopy.
ESTHER : Weik_2002_J.Synchrotron.Radiat_9_342
PubMedSearch : Weik_2002_J.Synchrotron.Radiat_9_342
PubMedID: 12409620

Title : Specific chemical and structural damage to proteins produced by synchrotron radiation - Weik_2000_Proc.Natl.Acad.Sci.U.S.A_97_623
Author(s) : Weik M , Ravelli RB , Kryger G , McSweeney S , Raves ML , Harel M , Gros P , Silman I , Kroon J , Sussman JL
Ref : Proceedings of the National Academy of Sciences of the United States of America , 97 :623 , 2000
Abstract : Radiation damage is an inherent problem in x-ray crystallography. It usually is presumed to be nonspecific and manifested as a gradual decay in the overall quality of data obtained for a given crystal as data collection proceeds. Based on third-generation synchrotron x-ray data, collected at cryogenic temperatures, we show for the enzymes Torpedo californica acetylcholinesterase and hen egg white lysozyme that synchrotron radiation also can cause highly specific damage. Disulfide bridges break, and carboxyl groups of acidic residues lose their definition. Highly exposed carboxyls, and those in the active site of both enzymes, appear particularly susceptible. The catalytic triad residue, His-440, in acetylcholinesterase, also appears to be much more sensitive to radiation damage than other histidine residues. Our findings have direct practical implications for routine x-ray data collection at high-energy synchrotron sources. Furthermore, they provide a direct approach for studying the radiation chemistry of proteins and nucleic acids at a detailed, structural level and also may yield information concerning putative "weak links" in a given biological macromolecule, which may be of structural and functional significance.
ESTHER : Weik_2000_Proc.Natl.Acad.Sci.U.S.A_97_623
PubMedSearch : Weik_2000_Proc.Natl.Acad.Sci.U.S.A_97_623
PubMedID: 10639129
Gene_locus related to this paper: torca-ACHE

Title : Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level - Millard_1999_Biochemistry_38_7032
Author(s) : Millard CB , Kryger G , Ordentlich A , Greenblatt HM , Harel M , Raves ML , Segall Y , Barak D , Shafferman A , Silman I , Sussman JL
Ref : Biochemistry , 38 :7032 , 1999
Abstract : Organophosphorus acid anhydride (OP) nerve agents are potent inhibitors which rapidly phosphonylate acetylcholinesterase (AChE) and then may undergo an internal dealkylation reaction (called "aging") to produce an OP-enzyme conjugate that cannot be reactivated. To understand the basis for irreversible inhibition, we solved the structures of aged conjugates obtained by reaction of Torpedo californica AChE (TcAChE) with diisopropylphosphorofluoridate (DFP), O-isopropylmethylphosponofluoridate (sarin), or O-pinacolylmethylphosphonofluoridate (soman) by X-ray crystallography to 2.3, 2.6, or 2.2 A resolution, respectively. The highest positive difference density peak corresponded to the OP phosphorus and was located within covalent bonding distance of the active-site serine (S200) in each structure. The OP-oxygen atoms were within hydrogen-bonding distance of four potential donors from catalytic subsites of the enzyme, suggesting that electrostatic forces significantly stabilize the aged enzyme. The active sites of aged sarin- and soman-TcAChE were essentially identical and provided structural models for the negatively charged, tetrahedral intermediate that occurs during deacylation with the natural substrate, acetylcholine. Phosphorylation with DFP caused an unexpected movement in the main chain of a loop that includes residues F288 and F290 of the TcAChE acyl pocket. This is the first major conformational change reported in the active site of any AChE-ligand complex, and it offers a structural explanation for the substrate selectivity of AChE.
ESTHER : Millard_1999_Biochemistry_38_7032
PubMedSearch : Millard_1999_Biochemistry_38_7032
PubMedID: 10353814
Gene_locus related to this paper: torca-ACHE

Title : Alternative Crystal Forms of Torpedo Californica Acetylcholinesterase -
Author(s) : Raves ML , Greenblatt HM , Kryger G , Nicolas A , Ravelli RB , Harel M , Kroon J , Silman I , Sussman JL
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :372 , 1998
PubMedID:

Title : Crystal Structures of Aged Phosphorylated and Phosphonylated Torpedo Californica Acetylcholinesterase -
Author(s) : Millard CB , Kryger G , Ordentlich A , Harel M , Raves ML , Greenblatt HM , Segall Y , Barak D , Shafferman A , Silman I , Sussman JL
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :425 , 1998
PubMedID:

Title : Crystal structure of Aged phosphorylated and phosphonylated Torpedo Californica Acetylcholinesterase -
Author(s) : Millard CB , Kryger G , Ordentlich A , Harel M , Raves ML , Greenblatt HM , Segall Y , Barak D , Shafferman A , Silman I , Sussman JL
Ref : In Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :425 , 1998
PubMedID:
Gene_locus related to this paper: torca-ACHE

Title : Static laue diffraction studies on acetylcholinesterase - Ravelli_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_1359
Author(s) : Ravelli RB , Raves ML , Ren Z , Bourgeois D , Roth M , Kroon J , Silman I , Sussman JL
Ref : Acta Crystallographica D Biol Crystallogr , 54 :1359 , 1998
Abstract : Acetylcholinesterase (AChE) is one of nature's fastest enzymes, despite the fact that its three-dimensional structure reveals its active site to be deeply sequestered within the molecule. This raises questions with respect to traffic of substrate to, and products from, the active site, which may be investigated by time-resolved crystallography. In order to address one aspect of the feasibility of performing time-resolved studies on AChE, a data set has been collected using the Laue technique on a trigonal crystal of Torpedo californica AChE soaked with the reversible inhibitor edrophonium, using a total X-ray exposure time of 24 ms. Electron-density maps obtained from the Laue data, which are of surprisingly good quality compared with similar maps from monochromatic data, show essentially the same features. They clearly reveal the bound ligand, as well as a structural change in the conformation of the active-site Ser200 induced upon binding.
ESTHER : Ravelli_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_1359
PubMedSearch : Ravelli_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_1359
PubMedID: 10089512
Gene_locus related to this paper: torca-ACHE

Title : Quaternary Structure of Tetrameric Acetylcholinesterase -
Author(s) : Raves ML , Giles K , Schrag JD , Schmid MF , Phillips JN, Jr. , Chiu W , Howard AJ , Silman I , Sussman JL
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :351 , 1998
PubMedID:
Gene_locus related to this paper: eleel-ACHE

Title : Crystal Structures of Aged Phosphorylated and Phosphonylated Torpedo Californica Acetylcholinesterase -
Author(s) : Millard CB , Kryger G , Ordentlich A , Harel M , Raves ML , Greenblatt HM , Segall Y , Barak D , Shafferman A , Silman I , Sussman JL
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :454 , 1998
PubMedID:

Title : Activity of Torpedo Californica Acetylcholinesterase in the Crystalline State -
Author(s) : Nicolas A , Millard CB , Raves ML , Ravelli RB , Kroon J , Silman I , Sussman JL
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :230 , 1998
PubMedID:

Title : Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A - Raves_1997_Nat.Struct.Biol_4_57
Author(s) : Raves ML , Harel M , Pang YP , Silman I , Kozikowski AP , Sussman JL
Ref : Nat Struct Biol , 4 :57 , 1997
Abstract : (-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE). The crystal structure of the complex of AChE with optically pure HupA at 2.5 A resolution shows an unexpected orientation for the inhibitor with surprisingly few strong direct interactions with protein residues to explain its high affinity. This structure is compared to the native structure of AChE devoid of any inhibitor as determined to the same resolution. An analysis of the affinities of structural analogues of HupA, correlated with their interactions with the protein, shows the importance of individual hydrophobic interactions between HupA and aromatic residues in the active-site gorge of AChE.
ESTHER : Raves_1997_Nat.Struct.Biol_4_57
PubMedSearch : Raves_1997_Nat.Struct.Biol_4_57
PubMedID: 8989325
Gene_locus related to this paper: torca-ACHE

Title : Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin - Marchot_1996_Prot.Sci_5_672
Author(s) : Marchot P , Ravelli RB , Raves ML , Bourne Y , Vellom DC , Kanter J , Camp S , Sussman JL , Taylor P
Ref : Protein Science , 5 :672 , 1996
Abstract : A soluble, monomeric form of acetylcholinesterase from mouse (mAChE), truncated at its carboxyl-terminal end, was generated from a cDNA encoding the glycophospholipid-linked form of the mouse enzyme by insertion of an early stop codon at position 549. Insertion of the cDNA behind a cytomegalovirus promoter and selection by aminoglycoside resistance in transfected HEK cells yielded clones secreting large quantities of mAChE into the medium. The enzyme sediments as a soluble monomer at 4.8 S. High levels of expression coupled with a one-step purification by affinity chromatography have allowed us to undertake a crystallographic study of the fasciculin-mAChE complex. Complexes of two distinct fasciculins, Fas1-mAChE and Fas2-mAChE, were formed prior to the crystallization and were characterized thoroughly. Single hexagonal crystals, up to 0.6 mm x 0.5 mm x 0.5 mm, grew spontaneously from ammonium sulfate solutions buffered in the pH 7.0 range. They were found by electrophoretic migration to consist entirely of the complex and diffracted to 2.8 A resolution. Analysis of initial X-ray data collected on Fas2-mAChE crystals identified the space group as P6(1)22 or P6(5)22 with unit cell dimensions a = b = 75.5 A, c = 556 A, giving a Vm value of 3.1 A3/Da (or 60% of solvent), consistent with a single molecule of Fas2-AChE complex (72 kDa) per asymmetric unit. The complex Fas1-mAChE crystallizes in the same space group with identical cell dimensions.
ESTHER : Marchot_1996_Prot.Sci_5_672
PubMedSearch : Marchot_1996_Prot.Sci_5_672
PubMedID: 8845756
Gene_locus related to this paper: mouse-ACHE

Title : Structures of Complexes of Acetylcholinesterase with Covalently and Non-Covalently Bound Inhibitors -
Author(s) : Sussman JL , Harel M , Raves ML , Quinn DM , Nair HK , Silman I
Ref : In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases , (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp. :59 , 1995
PubMedID:

Title : Studies on Partially Unfolded States of Torpedo californica Acetylcholinesterase -
Author(s) : Silman I , Kreimer DI , Shin I , Dolginova EA , Roth E , Goldfarb D , Szosenfogel R , Raves ML , Sussman JL , Borochov N , Weiner L
Ref : In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases , (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp. :77 , 1995
PubMedID:

Title : Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents -
Author(s) : Silman I , Harel M , Axelsen PH , Raves ML , Sussman JL
Ref : Biochemical Society Transactions , 22 :745 , 1994
PubMedID: 7821677

Title : A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials - Kreimer_1994_Biochemistry_33_14407
Author(s) : Kreimer DI , Dolginova EA , Raves ML , Sussman JL , Silman I , Weiner L
Ref : Biochemistry , 33 :14407 , 1994
Abstract : Chemical modification of Torpedo californica acetylcholinesterase by various sulfhydryl reagents results in its conversion to one of two principal states. One of these states, viz., that produced by disulfides and alkylating agents, is stable. The second state, produced by mercury derivatives, is metastable. At room temperature, it converts spontaneously, with a half-life of ca. 1 h, to a stable state similar to that produced by the disulfides and alkylating agents. Demodification of acetylcholinesterase freshly modified by mercurials, by its exposure to reduced glutathione, causes rapid release of the bound mercurial, with concomitant recovery of most of the enzymic activity of the native enzyme. In contrast, similar demodification of acetylcholinesterase modified by disulfides yields no detectable recovery of enzymic activity. Spectroscopic measurements, employing CD, intrinsic fluorescence, and binding of 1-anilino-8-naphthalenesulfonate, show that the state produced initially by mercurials is "native-like", whereas that produced by disulfides and alkylating agents, and after prolonged incubation of the mercurial-modified enzyme, is partially unfolded and displays many of the features of the "molten globule" state. Arrhenius plots show that the quasi-native state produced by organomercurials is separated by a low (5 kcal/mol) energy barrier from the native state, whereas the partially unfolded state is separated from the quasi-native state by a high energy barrier (ca. 50 kcal/mol). Comparison of the 3D structures of native acetylcholinesterase and of a heavy-atom derivative obtained with HgAc2 suggests that the mercurial-modified enzyme may be stabilized by additional interactions of the mercury atom attached to the free thiol group of Cys231, specifically with Ser228O gamma with the main-chain nitrogen and carbonyl oxygen of the same serine residue.
ESTHER : Kreimer_1994_Biochemistry_33_14407
PubMedSearch : Kreimer_1994_Biochemistry_33_14407
PubMedID: 7981200
Gene_locus related to this paper: torca-ACHE