1nyc | pdb_00001nyc
Staphostatins resemble lipocalins, not cystatins in fold.
| |||||||||||||
| 1nyc, resolution 1.40Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CL and SO4 | ||||||||||||
| Gene: | staphostatin B (sspC) (Staphylococcus aureus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
Page seeded by OCA on Thu Mar 20 13:03:22 2008
