Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rzychon M, Filipek R, Sabat A, Kosowska K, Dubin A, Potempa J, Bochtler M. Staphostatins resemble lipocalins, not cystatins in fold. Protein Sci. 2003 Oct;12(10):2252-6. PMID:14500882
