title: Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL.
abstract: 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.
authors: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
authors: Tavarekere S
authors: TS
authors: Girish
authors: Vivek
authors: V
authors: B
authors: Melwin
authors: M
authors: Colaco
authors: Sandra
authors: S
authors: Misquith
authors: B
authors: B
authors: Gopal
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D055624:Methicillin-Resistant Staphylococcus aureus / Q000201:enzymology*; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D000581:Amidohydrolases
keywords: M20D peptidases; Mn2+-dependent dipeptidases; amidohydrolases
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