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PDBsum entry 1srp
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Hydrolase (metalloprotease)
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PDB id
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1srp
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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K.Hamada,
Y.Hata,
Y.Katsuya,
H.Hiramatsu,
T.Fujiwara,
Y.Katsube.
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Ref.
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J Biochem (tokyo), 1996,
119,
844-851.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Structural studies of serratia protease by X-Ray analysis
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Authors
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K.Hamada,
H.Hiramatsu,
T.Fujiwara,
Y.Katsuya,
Y.Hata,
Y.Katsube.
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Ref.
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photon factory activity, 1992,
10,
125.
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Secondary reference #2
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Title
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Preliminary X-Ray studies on serratia protease.
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Authors
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Y.Katsuya,
K.Hamada,
Y.Hata,
N.Tanaka,
M.Sato,
Y.Katsube,
K.Kakiuchi,
K.Miyata.
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Ref.
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J Biochem (tokyo), 1985,
98,
1139-1142.
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PubMed id
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