1h8y | pdb_00001h8y
CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-13 IN COMPLEX WITH MEROPENEM
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Overview
The therapeutic problems posed by class D beta-lactamases, a family of, serine enzymes that hydrolyse beta-lactam antibiotics following an, acylation-deacylation mechanism, are increased by the very low level of, sensitivity of these enzymes to beta-lactamase inhibitors. To gain, structural and mechanistic insights to aid the design of new inhibitors, we have determined the crystal structure of OXA-13 from Pseudomonas, aeruginosa in the apo form and in complex with the carbapenem meropenem., The native form consisted of a dimer displaying an overall organisation, similar to that found in the closely related enzyme OXA-10. In the, acyl-enzyme complex, the positioning of the antibiotic appeared to be, ensured mainly by (i) the covalent acyl bond and (ii) a strong salt-bridge, involving the ... [(full description)]
About this Structure
1H8Y is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with SO4 and MER as [ligands]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].
Reference
Crystal structures of the class D beta-lactamase OXA-13 in the native form and in complex with meropenem., Pernot L, Frenois F, Rybkine T, L'Hermite G, Petrella S, Delettre J, Jarlier V, Collatz E, Sougakoff W, J Mol Biol. 2001 Jul 20;310(4):859-74. PMID:11453693
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