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PDBsum entry 1mee
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Complex(serine proteinase-inhibitor)
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PDB id
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1mee
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Contents |
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* Residue conservation analysis
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Enzyme class 2:
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Chain A:
E.C.3.4.21.62
- subtilisin.
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Reaction:
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Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
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Enzyme class 3:
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Chain I:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Acta Crystallogr B
47:707-730
(1991)
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PubMed id:
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Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.
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Z.Dauter,
C.Betzel,
N.Genov,
N.Pipon,
K.S.Wilson.
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ABSTRACT
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The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has
been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical
leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and
beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to
2.0 A have been recorded on film from a single crystal. The orientation and
position of the complex in the unit cell have been established using the refined
coordinates of subtilisin Carlsberg and of eglin-C as independent models. The
structure of the complex has been refined by restrained least-squares
minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude
of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water
molecules. The structure is discussed in terms of its physicochemical properties
in solution and its relation to other Bacillus subtilisins.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Vévodová,
M.Gamble,
G.Künze,
A.Ariza,
E.Dodson,
D.D.Jones,
and
K.S.Wilson
(2010).
Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.
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Structure,
18,
744-755.
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PDB codes:
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J.S.Fetrow,
S.T.Knutson,
and
M.H.Edgell
(2006).
Mutations in alpha-helical solvent-exposed sites of eglin c have long-range effects: evidence from molecular dynamics simulations.
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Proteins,
63,
356-372.
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A.J.Bordner,
and
R.Abagyan
(2005).
Statistical analysis and prediction of protein-protein interfaces.
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Proteins,
60,
353-366.
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C.K.Brown,
Z.Y.Gu,
Y.V.Matsuka,
S.S.Purushothaman,
L.A.Winter,
P.P.Cleary,
S.B.Olmsted,
D.H.Ohlendorf,
and
C.A.Earhart
(2005).
Structure of the streptococcal cell wall C5a peptidase.
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Proc Natl Acad Sci U S A,
102,
18391-18396.
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PDB code:
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J.P.Turkenburg,
and
E.J.Dodson
(1996).
Modern developments in molecular replacement.
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Curr Opin Struct Biol,
6,
604-610.
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G.Lange,
C.Betzel,
S.Branner,
and
K.S.Wilson
(1994).
Crystallographic studies of Savinase, a subtilisin-like proteinase, at pH 10.5.
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Eur J Biochem,
224,
507-518.
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K.Huang,
N.C.Strynadka,
V.D.Bernard,
R.J.Peanasky,
and
M.N.James
(1994).
The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase.
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Structure,
2,
679-689.
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PDB code:
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E.Meyer
(1992).
Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications.
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Protein Sci,
1,
1543-1562.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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