1k9b
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(New page: 200px<br /><applet load="1k9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k9b, resolution 2.8Å" /> '''Crystal structure of ...)
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Revision as of 16:51, 20 November 2007
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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
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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