Han GW

References (3)

Title : Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima - Levisson_2012_Proteins_80_1545
Author(s) : Levisson M , Han GW , Deller MC , Xu Q , Biely P , Hendriks S , Ten Eyck LF , Flensburg C , Roversi P , Miller MD , McMullan D , von Delft F , Kreusch A , Deacon AM , Van der Oost J , Lesley SA , Elsliger MA , Kengen SW , Wilson IA
Ref : Proteins , 80 :1545 , 2012
Abstract : TM0077 from Thermotoga maritima is a member of the carbohydrate esterase family 7 and is active on a variety of acetylated compounds, including cephalosporin C. TM0077 esterase activity is confined to short-chain acyl esters (C2-C3), and is optimal around 100degC and pH 7.5. The positional specificity of TM0077 was investigated using 4-nitrophenyl--D-xylopyranoside monoacetates as substrates in a -xylosidase-coupled assay. TM0077 hydrolyzes acetate at positions 2, 3, and 4 with equal efficiency. No activity was detected on xylan or acetylated xylan, which implies that TM0077 is an acetyl esterase and not an acetyl xylan esterase as currently annotated. Selenomethionine-substituted and native structures of TM0077 were determined at 2.1 and 2.5 resolution, respectively, revealing a classicalpha/beta-hydrolase fold. TM0077 assembles into a doughnut-shaped hexamer with small tunnels on either side leading to an inner cavity, which contains the six catalytic centers. Structures of TM0077 with covalently bound phenylmethylsulfonyl fluoride and paraoxon were determined to 2.4 and 2.1 , respectively, and confirmed that both inhibitors bind covalently to the catalytic serine (Ser188). Upon binding of inhibitor, the catalytic serine adopts an altered conformation, as observed in other esterase and lipases, and supports a previously proposed catalytic mechanism in which Ser hydroxyl rotation prevents reversal of the reaction and allows access of a water molecule for completion of the reaction.
ESTHER : Levisson_2012_Proteins_80_1545
PubMedSearch : Levisson_2012_Proteins_80_1545
PubMedID: 22411095
Gene_locus related to this paper: thema-TM0077

Title : Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution -
Author(s) : Zubieta C , Krishna SS , McMullan D , Miller MD , Abdubek P , Agarwalla S , Ambing E , Astakhova T , Axelrod HL , Carlton D , Chiu HJ , Clayton T , Deller M , DiDonato M , Duan L , Elsliger MA , Grzechnik SK , Hale J , Hampton E , Han GW , Haugen J , Jaroszewski L , Jin KK , Klock HE , Knuth MW , Koesema E , Kumar A , Marciano D , Morse AT , Nigoghossian E , Oommachen S , Reyes R , Rife CL , van den Bedem H , Weekes D , White A , Xu Q , Hodgson KO , Wooley J , Deacon AM , Godzik A , Lesley SA , Wilson IA
Ref : Proteins , 68 :999 , 2007
PubMedID: 17546672
Gene_locus related to this paper: bacce-BC4730

Title : Crystal structure of an alpha\/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution -
Author(s) : Arndt JW , Schwarzenbacher R , Page R , Abdubek P , Ambing E , Biorac T , Canaves JM , Chiu HJ , Dai X , Deacon AM , DiDonato M , Elsliger MA , Godzik A , Grittini C , Grzechnik SK , Hale J , Hampton E , Han GW , Haugen J , Hornsby M , Klock HE , Koesema E , Kreusch A , Kuhn P , Jaroszewski L , Lesley SA , Levin I , McMullan D , McPhillips TM , Miller MD , Morse A , Moy K , Nigoghossian E , Ouyang J , Peti WS , Quijano K , Reyes R , Sims E , Spraggon G , Stevens RC , van den Bedem H , Velasquez J , Vincent J , von Delft F , Wang X , West B , White A , Wolf G , Xu Q , Zagnitko O , Hodgson KO , Wooley J , Wilson IA
Ref : Proteins , 58 :755 , 2005
PubMedID: 15624212
Gene_locus related to this paper: yeast-YDR428C