Structure 2GOP The beta-propeller domain of the Trilobed protease from Pyrococcus furiosus reveals an open velcro topology does not includes the alpha/beta hydrolase domain
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Archaea: NE > Euryarchaeota: NE > Thermococci: NE > Thermococcales: NE > Thermococcaceae: NE > Pyrococcus: NE > Pyrococcus furiosus: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MSSIEWNEKTFAKFAYLSDPRTKGELVAYVLTKANLKDNKYENTIVIENL KNNARRFIENATMPRISPDGKKIAFMRANEEKKVSEIWVADLETLSSKKI LEAKNIRSLEWNEDSRKLLIVGFKRREDEDFIFEDDVPAWFDDLGFFDGE KTTFWIFDTESEEVIEEFEKPRFSSGIWHRDKIVVNVPHREIIPQYFKFW DIYIWEDGKEEKMFEKVSFYAVDSDGERILLYGKPEKKYMSEHNKLYIYD GKEVMGILDEVDRGVGQAKIKDGKVYFTLFEEGSVNLYIWDGEIKPIAKG RHWIMGFDVDEIVVYLKETATRLRELFTWDGEEKQLTDYNDPIFAKLKTF EPVHFRYKSLDLEIDGWYMKPELKEGEKAPVIVFVHGGPKGMYGYYFKYE MQLMAAKGYYIVYVNPRGSNGYSEDFALRVLTRTGLEDFQDILNGIEEFL KLEPQADRERIGITGISYGGYMTNWALTQSDLFKAGISENGISYWLTSYA FSDIGLWFDKEVIGENPLENENFRRLSPLFYAKNVKAPILLIHSLEDYRC PLDQSLMFYHVLKDLGKEAYIAIFKRGAHGHSIRGQPRHRMKRYKLFVEF FERKLKKYEEGFPIEKILKE
Reference
Title: The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology Bosch J, Tamura T, Tamura N, Baumeister W, Essen LO Ref: Acta Crystallographica D Biol Crystallogr, 63:179, 2007 : PubMed
In the proteolytic pathway of prokaryotic and eukaryotic organisms, proteins tagged for proteolysis are firstly shredded into smaller peptides by compartmentalized proteases such as the proteasome complex. Accordingly, a variety of downstream proteases have evolved to further hydrolyze these peptides to the level of free amino acids. In the search for such downstream proteases, a high-molecular-weight protease complex called trilobed protease (TLP) was recently discovered in the archaeon Pyroccocus furiosus. The crystal structure of the N-terminal beta-propeller domain of the trilobed protease at 2 A resolution shows that the trilobed protease utilizes this accessory domain to control substrate access to the active site. Modelling of the intact TLP monomer suggests that this protease has an additional side entrance to its active site as in the DPP-IV or tricorn protease complexes.