1nyc | pdb_00001nyc

Staphostatins resemble lipocalins, not cystatins in fold.

spinqualitylabelsall models 1nyc, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nyc is a 2 chain structure with sequence from Staaw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, SO4 Gene: staphostatin B (sspC) (STAAW) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SSPC_STAAW] Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology (By similarity). Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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