1dy6
From Proteopedia
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STRUCTURE OF THE IMIPENEM-HYDROLYZING BETA-LACTAMASE SME-1
Overview
The structure of the beta-lactamase SME-1 from Serratia marcescens, a, class A enzyme characterized by its significant activity against imipenem, has been determined to 2.13 A resolution. The overall structure of SME-1, is similar to that of other class A beta-lactamases. In the active-site, cavity, most of the residues found in SME-1 are conserved among class A, beta-lactamases, except at positions 104, 105 and 237, where a tyrosine, a, histidine and a serine are found, respectively, and at position 238, which, is occupied by a cysteine forming a disulfide bridge with the other, cysteine residue located at position 69. The crucial role played by this, disulfide bridge in SME-1 was confirmed by site-directed mutagenesis of, Cys69 to Ala, which resulted in a mutant unable to confer ... [(full description)]
About this Structure
1DY6 is a [Single protein] structure of sequence from [Serratia marcescens]. Active as [Hydrolase], with EC number [3.5.2.6]. Structure known Active Sites: ASA and ASB. Full crystallographic information is available from [OCA].
Reference
Structure of the imipenem-hydrolyzing class A beta-lactamase SME-1 from Serratia marcescens., Sougakoff W, L'Hermite G, Pernot L, Naas T, Guillet V, Nordmann P, Jarlier V, Delettre J, Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):267-74. Epub 2002, Jan 24. PMID:11807251
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