4ewt

The crystal structure of a putative aminohydrolase from methicillin resistant Staphylococcus aureus

spinqualitylabelsall models 4ewt, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ewt is a 4 chain structure with sequence from Staphylococcus aureus subsp. aureus COL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MN, PE7, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2WZV8_STAAC Publication Abstract from PubMed Staphylococcus aureus is an opportunistic pathogen that rapidly acquires resistance to frontline antibiotics. The characterization of novel protein targets from this bacterium is thus an important step towards future therapeutic strategies. Here, the crystal structure of an amidohydrolase, SACOL0085, from S. aureus COL is described. SACOL0085 is a member of the M20D family of peptidases. Unlike other M20D peptidases, which are either monomers or dimers, SACOL0085 adopts a butterfly-shaped homotetrameric arrangement with extensive intersubunit interactions. Each subunit of SACOL0085 contains two Mn(2+) ions at the active site. A conserved cysteine residue at the active site distinguishes M20D peptidases from other M20 family members. This cysteine, Cys103, serves as bidentate ligand coordinating both Mn(2+) ions in SACOL0085. Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL.,Girish TS, B V, Colaco M, Misquith S, Gopal B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Feb 1;69(Pt 2):103-8. doi:, 10.1107/S1744309112049822. Epub 2013 Jan 30. PMID:23385746 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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