1k9b
From Proteopedia
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- | [[Image:1k9b.jpg|left|200px]] | + | [[Image:1k9b.jpg|left|200px]] |
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- | '''Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation''' | + | {{Structure |
+ | |PDB= 1k9b |SIZE=350|CAPTION= <scene name='initialview01'>1k9b</scene>, resolution 2.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1K9B is a [ | + | 1K9B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9B OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation., Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P, Eur J Biochem. 1996 Nov 15;242(1):122-31. PMID:[http:// | + | Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation., Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P, Eur J Biochem. 1996 Nov 15;242(1):122-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8954162 8954162] |
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tripple-stranded beta hairpin]] | [[Category: tripple-stranded beta hairpin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:14:19 2008'' |
Revision as of 10:14, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation
Overview
The Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. & Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The proximity of Met27 and Gln48 in the X-ray structure contradicts the solution structure, in which these two side chains point away from each other. The significant effect of a Met27-->Ile replacement on the inhibitory activity of the chymotrypsin-reactive subdomain agrees with the X-ray structure. Exposed hydrophobic patches, the presence of charged amino acid residues, and the presence of water molecules in the protein interior are in contrast to standard proteins that comprise a hydrophobic core and exposed polar amino acids.
About this Structure
1K9B is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation., Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P, Eur J Biochem. 1996 Nov 15;242(1):122-31. PMID:8954162
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