1k9b
From Proteopedia
(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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| - | [[Image:1k9b.jpg|left|200px]]<br /><applet load="1k9b" size=" | + | [[Image:1k9b.jpg|left|200px]]<br /><applet load="1k9b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k9b, resolution 2.8Å" /> | caption="1k9b, resolution 2.8Å" /> | ||
'''Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation'''<br /> | '''Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Bowman-Birk inhibitor from soybean is a small protein that contains a | + | 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== | ==About this Structure== | ||
| - | 1K9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http:// | + | 1K9B is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ermler, U.]] | [[Category: Ermler, U.]] | ||
| - | [[Category: Essen, L | + | [[Category: Essen, L O.]] |
[[Category: Flecker, P.]] | [[Category: Flecker, P.]] | ||
| - | [[Category: Kim, Y | + | [[Category: Kim, Y M.]] |
| - | [[Category: Voss, R | + | [[Category: Voss, R H.]] |
[[Category: Wenzl, G.]] | [[Category: Wenzl, G.]] | ||
[[Category: double-headed]] | [[Category: double-headed]] | ||
[[Category: tripple-stranded beta hairpin]] | [[Category: tripple-stranded beta hairpin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:33 2008'' |
Revision as of 11:31, 21 February 2008
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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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