1nyc
From Proteopedia
(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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| - | [[Image:1nyc.jpg|left|200px]]<br /><applet load="1nyc" size=" | + | [[Image:1nyc.jpg|left|200px]]<br /><applet load="1nyc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nyc, resolution 1.40Å" /> | caption="1nyc, resolution 1.40Å" /> | ||
'''Staphostatins resemble lipocalins, not cystatins in fold.'''<br /> | '''Staphostatins resemble lipocalins, not cystatins in fold.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Staphostatins are the endogenous inhibitors of the major secreted cysteine | + | 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== | ==About this Structure== | ||
| - | 1NYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with CL and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: staphostatin b]] | [[Category: staphostatin b]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:23 2008'' |
Revision as of 12:11, 21 February 2008
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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 and 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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