2uzj | pdb_00002uzj

CRYSTAL STRUCTURE OF THE MATURE STREPTOCOCCAL CYSTEINE PROTEASE, MSPEB

spinqualitylabelsall models 2uzj, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2uzj is a 2 chain structure with sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: E64 Activity: Streptopain, with EC number 3.4.22.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SPEB_STRP6] Important streptococcal virulence factor which cleaves human fibronectin and degrades vitronectin. Also cleaves human IL1B precursor to form biologically active IL1B. Can induce apoptosis in human monocytes and epithelial cells in vitro, and reduces phagocytic activity in monocytic cells. Thus, may play a role in bacterial colonization, invasion, and inhibition of wound healing. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Invasive infections of Streptococcus pyogenes are dependent on the cysteine protease streptococcal pyrogenic exotoxin B. Previous structures of the enzyme have not disclosed the proper active-site configuration. Here, the crystal structure of the mature enzyme is presented to 1.55 A, disclosing a homodimer. A serine from one subunit inserts into the active site of the other to donate to the oxyanion hole and coordinates the ligand proximal to the active-site cysteine. Dimerization is unique to the mature form and is clearly a prerequisite for catalysis. The present structure supports a tripartite switch system that is triggered upon dimerization and substrate binding: (1) liberation of the active-site histidine from an inactive configuration, (2) relocation of residues blocking the substrate binding pockets and (3) repositioning of two active-site tryptophans to settle in the active configuration. Based on the present structure, the active site of clan CA cysteine proteases is expanded and a detailed mechanism of the deacylation mechanism is proposed. The results may have applications for the development of protease inhibitors specific to bacterial cysteine proteases. Structure of the mature Streptococcal cysteine protease exotoxin mSpeB in its active dimeric form.,Olsen JG, Dagil R, Niclasen LM, Sorensen OE, Kragelund BB J Mol Biol. 2009 Oct 30;393(3):693-703. Epub 2009 Aug 25. PMID:19712682 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exotoxin

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