1NYC

Staphostatins resemble lipocalins, not cystatins in fold.

Summary for 1NYC

• Entry DOI: 10.2210/pdb1nyc/pdb
• Descriptor: cysteine protease inhibitor, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: staphostatin b, sspc, cysteine protease inhibitor, hydrolase inhibitor
• Biological source: Staphylococcus aureus subsp. aureus
• Cellular location: Cytoplasm (By similarity): Q7A189
• Total number of polymer chains: 2
• Total formula weight: 26316.21

Authors

Rzychon, M.,Filipek, R.,Sabat, A.,Kosowska, K.,Dubin, A.,Potempa, J.,Bochtler, M. (deposition date: 2003-02-12, release date: 2003-09-30, Last modification date: 2024-02-14)

Primary citation

Rzychon, M.,Filipek, R.,Sabat, A.,Kosowska, K.,Dubin, A.,Potempa, J.,Bochtler, M.
Staphostatins resemble lipocalins, not cystatins in fold.
Protein Sci., 12:2252-2256, 2003

PubMed Abstract: 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.

PubMed: 14500882
DOI: 10.1110/ps.03247703

Experimental method

X-RAY DIFFRACTION (1.4 Å)