1PXV
The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease
Summary for 1PXV
| Entry DOI | 10.2210/pdb1pxv/pdb |
| Related | 1CV8 1NYC |
| Descriptor | cysteine protease, cysteine protease Inhibitor, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | cysteine protease inhibitor, hydrolase |
| Biological source | Staphylococcus aureus More |
| Cellular location | Secreted (By similarity): Q70UQ8 Cytoplasm: Q9EYW6 |
| Total number of polymer chains | 4 |
| Total formula weight | 68812.79 |
| Authors | Filipek, R.,Rzychon, M.,Oleksy, A.,Gruca, M.,Dubin, A.,Potempa, J.,Bochtler, M. (deposition date: 2003-07-07, release date: 2003-10-21, Last modification date: 2023-08-16) |
| Primary citation | Filipek, R.,Rzychon, M.,Oleksy, A.,Gruca, M.,Dubin, A.,Potempa, J.,Bochtler, M. The Staphostatin-Staphopain Complex: A FORWARD BINDING INHIBITOR IN COMPLEX WITH ITS TARGET CYSTEINE PROTEASE. J.Biol.Chem., 278:40959-40966, 2003 Cited by PubMed Abstract: Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel with statistically significant similarity to lipocalins, but not to cystatins. We now present the 1.8-A crystal structure of staphostatin B in complex with an inactive mutant of its target protease. The complex is held together through extensive interactions and buries a total surface area of 2300 A2. Unexpectedly for a cysteine protease inhibitor, staphostatin B binds to staphopain B in an almost substrate-like manner. The inhibitor polypeptide chain runs through the protease active site cleft in the forward direction, with residues IG-TS in P2 to P2' positions. Both in the free and complexed forms, the P1 glycine residue of the inhibitor is in a main chain conformation only accessible to glycines. Mutations in this residue lead to a loss of affinity of the inhibitor for protease and convert the inhibitor into a substrate. PubMed: 12874290DOI: 10.1074/jbc.M302926200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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