spacer
spacer

PDBsum entry 3sgb

Go to PDB code: 
Top Page protein Protein-protein interface(s) links
Complex(serine proteinase-inhibitor) PDB id
3sgb
Contents
Protein chains
185 a.a. *
50 a.a. *
Waters ×182
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure of the complex of streptomyces griseus protease b and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.
Authors R.J.Read, M.Fujinaga, A.R.Sielecki, M.N.James.
Ref. Biochemistry, 1983, 22, 4420-4433. [DOI no: 10.1021/bi00288a012]
PubMed id 6414511
Abstract
The structure of the complex between the serine protease Streptomyces griseus protease B (SGPB) and the third domain of the Kazal-type ovomucoid inhibitor from turkey has been solved at 1.8-A resolution and refined to a conventional R factor of 0.125. As others have reported previously for analogous complexes of proteases and protein inhibitors, the inhibitor binds in a fashion similar to that of a substrate; it is not cleaved, but there is a close approach (2.7 A) of the active site nucleophile Ser-195 O gamma to the carbonyl carbon of the reactive peptide bond of the inhibitor. Contrary to the structural reports regarding the other enzyme-inhibitor complexes, we conclude that there is no evidence for a significant distortion of this peptide bond from planarity. The mechanism of inhibition can be understood in terms of the equilibrium thermodynamic parameters Ka, the enzyme-inhibitor association constant, and Khyd, the equilibrium constant for inhibitor hydrolysis. These thermodynamic parameters can be rationalized in terms of the observed structure.
Secondary reference #1
Title Crystal and molecular structures of the complex of alpha-Chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 a resolution.
Authors M.Fujinaga, A.R.Sielecki, R.J.Read, W.Ardelt, M.Laskowski, M.N.James.
Ref. J Mol Biol, 1987, 195, 397-418.
PubMed id 3477645
Abstract
Secondary reference #2
Title Refined crystal structure of the molecular complex of streptomyces griseus protease b, A serine protease, With the third domain of the ovomucoid inhibitor from turkey.
Authors M.Fujinaga, R.J.Read, A.Sielecki, W.Ardelt, M.Laskowski, M.N.James.
Ref. Proc Natl Acad Sci U S A, 1982, 79, 4868-4872. [DOI no: 10.1073/pnas.79.16.4868]
PubMed id 6750612
Full text Abstract
Secondary reference #3
Title Crystal structure studies and inhibition kinetics of tripeptide chloromethyl ketone inhibitors with streptomyces griseus protease b.
Authors M.N.James, G.D.Brayer, L.T.Delbaere, A.R.Sielecki, A.Gertler.
Ref. J Mol Biol, 1980, 139, 423-438. [DOI no: 10.1016/0022-2836(80)90139-4]
PubMed id 6777499
Full text Abstract
Figure 2.
RI Phe
Figure 5.
FIG. 5. Stereo-drawing of the inhibitors: (a) BocGLF and (b) BocAGF bound in the active site of SGPB, as interpreted from the 2.8 A resolution difference electron density maps of their respec- tive complexes (Fig. 2). Polypeptide main-chain bonding of the enzyme and all interatomic bonds of the bound inhibitors are indicated by solid black bonds All oxygen atoms are dis- tinguished by solid black circles. Hydrogen bnds to active site residues and the boun inhibitors are indicated by thin broken lines. For the BocGLF-SGPB complex, the new position of the side- chain of Tyrl71 is shown, while the original native conformation of this residue is indicated by broken lines.
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #4
Title The 2.8 a resolution structure of streptomyces griseus protease b and its homology with alpha-Chymotrypsin and streptomyces griseus protease a.
Authors L.T.Delbaere, G.D.Brayer, M.N.James.
Ref. Can J Biochem, 1979, 57, 135-144.
PubMed id 110426
Abstract
Secondary reference #5
Title Amino acid sequence alignment of bacterial and mammalian pancreatic serine proteases based on topological equivalences.
Authors M.N.James, L.T.Delbaere, G.D.Brayer.
Ref. Can J Biochem, 1978, 56, 396-402.
PubMed id 96920
Abstract
Secondary reference #6
Title Relationship between the structures and activities of some microbial serine proteases. II. Comparison of the tertiary structures of microbial and pancreatic serine proteases
Author M.N.G.James.
Ref. miami winter symp, 1976, 11, 125.
Secondary reference #7
Title Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes.
Authors L.T.Delbaere, W.L.Hutcheon, M.N.James, W.E.Thiessen.
Ref. Nature, 1975, 257, 758-763.
PubMed id 1186854
Abstract
Secondary reference #8
Title The 4.5 angstrom resolution structure of a bacterial serine protease from streptomyces griseus.
Authors P.W.Codding, L.T.Delbaere, K.Hayakawa, W.L.Hutcheon, M.N.James, L.Jurásek.
Ref. Can J Biochem, 1974, 52, 208-220.
PubMed id 4208242
Abstract
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer