1srp
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STRUCTURAL ANALYSIS OF SERRATIA PROTEASE
OverviewOverview
The crystal structure of Serratia protease from Serratia sp. E-15 was, solved by the single isomorphous replacement method supplemented with, anomalous scattering effects from both the Zn atom in the native crystal, and the Sm atom in the derivative crystal, and refined at 2.0 A resolution, to a crystallographic R-factor of 0.194. The enzyme consists of N-terminal, catalytic and C-terminal beta-sandwich domains, as observed in alkaline, protease from Pseudomonas aeruginosa IFO3080. The catalytic domain with a, five-stranded antiparallel beta-sheet and five alpha-helices shares a, basically common folding topology with those of other zinc, metalloendoproteases. The catalytic zinc ion at the bottom of the active, site cleft is ligated by His176, His180, His186, Tyr216, and a water, molecule in a distorted trigonalbipyramidal manner. The C-terminal domain, is a beta-strand-rich domain containing eighteen beta-strands and a short, alpha-helix, and has seven Ca2+ ions bound to calcium binding loops. An, unusual beta-sheet coil motif is observed in this domain, where the, beta-strands and calcium binding loops are alternately incorporated into, an elliptical right-handed spiral so as to form a two-layer untwisted, beta-sandwich structure. The Ca2+ ions in the C-terminal domain seem to be, very important for the folding and stability of the beta-sheet coil, structure.
About this StructureAbout this Structure
1SRP is a Single protein structure of sequence from Serratia sp. with CA and ZN as ligands. Active as Serralysin, with EC number 3.4.24.40 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0 A resolution., Hamada K, Hata Y, Katsuya Y, Hiramatsu H, Fujiwara T, Katsube Y, J Biochem (Tokyo). 1996 May;119(5):844-51. PMID:8797082
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