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PDBsum entry 1sgq
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Complex (serine protease/inhibitor)
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PDB id
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1sgq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Water molecules participate in proteinase-Inhibitor interactions: crystal structures of leu18, Ala18, And gly18 variants of turkey ovomucoid inhibitor third domain complexed with streptomyces griseus proteinase b.
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Authors
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K.Huang,
W.Lu,
S.Anderson,
M.Laskowski,
M.N.James.
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Ref.
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Protein Sci, 1995,
4,
1985-1997.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
91%.
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Abstract
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Crystal structures of the complexes of Streptomyces griseus proteinase B (SGPB)
with three P1 variants of turkey ovomucoid inhibitor third domain (OMTKY3),
Leu18, Ala18, and Gly18, have been determined and refined to high resolution.
Comparisons among these structures and of each with native, uncomplexed SGPB
reveal that each complex features a unique solvent structure in the S1 binding
pocket. The number and relative positions of water molecules bound in the S1
binding pocket vary according to the size of the side chain of the P1 residue.
Water molecules in the S1 binding pocket of SGPB are redistributed in response
to the complex formation, probably to optimize hydrogen bonds between the enzyme
and the inhibitor. There are extensive water-mediated hydrogen bonds in the
interfaces of the complexes. In all complexes, Asn 36 of OMTKY3 participates in
forming hydrogen bonds, via water molecules, with residues lining the S1 binding
pocket of SGPB. For a homologous series of aliphatic straight side chains,
Gly18, Ala18, Abu18, Ape18, and Ahp18 variants, the binding free energy is a
linear function of the hydrophobic surface area buried in the interface of the
corresponding complexes. The resulting constant of proportionality is 34.1 cal
mol-1 A-2. These structures confirm that the binding of OMTKY3 to the preformed
S1 pocket in SGPB involves no substantial structural disturbances that commonly
occur in the site-directed mutagenesis studies of interior residues in other
proteins, thus providing one of the most reliable assessments of the
contribution of the hydrophobic effect to protein-complex stability.
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Secondary reference #1
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Title
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Structure of the complex of streptomyces griseus protease b and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.
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Authors
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R.J.Read,
M.Fujinaga,
A.R.Sielecki,
M.N.James.
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Ref.
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Biochemistry, 1983,
22,
4420-4433.
[DOI no: ]
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PubMed id
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