4EWT
The crystal structure of a putative aminohydrolase from methicillin resistant Staphylococcus aureus
Summary for 4EWT
| Entry DOI | 10.2210/pdb4ewt/pdb |
| Descriptor | Peptidase, M20/M25/M40 family, MANGANESE (II) ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | peptidase, m20/m25/m40 family, hydrolase, mn/zn binding |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 174183.83 |
| Authors | Girish, T.S.,Vivek, B.,Colaco, M.,Misquith, S.,Gopal, B. (deposition date: 2012-04-27, release date: 2013-02-20, Last modification date: 2023-11-08) |
| Primary citation | Girish, T.S.,Vivek, B.,Colaco, M.,Misquith, S.,Gopal, B. Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL Acta Crystallogr.,Sect.F, 69:103-108, 2013 Cited by PubMed 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. PubMed: 23385746DOI: 10.1107/S1744309112049822 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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