Staphostatins resemble lipocalins, not cystatins in fold.
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ABSTRACT:
SUBMITTER: Rzychon M
PROVIDER: S-EPMC2366914 | biostudies-literature | 2003 Oct
REPOSITORIES: biostudies-literature
Publications
Staphostatins resemble lipocalins, not cystatins in fold.
Rzychon Malgorzata M Filipek Renata R Sabat Artur A Kosowska Klaudia K Dubin Adam A Potempa Jan J Bochtler Matthias M
Protein science : a publication of the Protein Society 20031001 10
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 bind ...[more]
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