1nyc
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(New page: 200px<br /><applet load="1nyc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nyc, resolution 1.40Å" /> '''Staphostatins resemb...)
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Revision as of 20:32, 20 November 2007
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Staphostatins resemble lipocalins, not cystatins in fold.
Overview
Staphostatins are the endogenous inhibitors of the major secreted cysteine, proteases of Staphylococcus aureus, the staphopains. Here, we present the, 1.4 A crystal structure of staphostatin B and show that the fold can be, described as a fully closed, highly sheared eight-stranded beta-barrel., Thus, staphostatin B is related to beta-barrel domains that are involved, in the inhibition or regulation of proteases of various catalytic types, and to the superfamily of lipocalins/cytosolic fatty acid binding, proteins. Unexpectedly for a cysteine protease inhibitor, staphostatin B, is not significantly similar to cystatins.
About this Structure
1NYC is a Single protein structure of sequence from Staphylococcus aureus with CL and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Staphostatins resemble lipocalins, not cystatins in fold., Rzychon M, Filipek R, Sabat A, Kosowska K, Dubin A, Potempa J, Bochtler M, Protein Sci. 2003 Oct;12(10):2252-6. PMID:14500882
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