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Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL

Girish, Tavarekere S and Vivek, B and Colaco, Melwin and Misquith, Sandra and Gopal, B (2013) Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL. In: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 69 (Part 2). pp. 103-108.

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Official URL: http://dx.doi.org/10.1107/S1744309112049822

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 Mn2+ 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 Mn2+ ions in SACOL0085.

Item Type: Journal Article
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Additional Information: Copyright for this article belongs to WILEY-BLACKWELL, USA
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 07 Mar 2013 12:18
Last Modified: 07 Mar 2013 12:18
URI: http://eprints.iisc.ernet.in/id/eprint/45940

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