Abstract：
:The beta-lactamases are involved in bacterial resistance to penicillin and related compounds. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are thus becoming of major clinical importance. The structures of the Zn-beta-lactamase from Fluoribacter gormanii (FEZ-1) in the native and in the complex form are reported here. FEZ-1 is a monomeric enzyme, which possesses two zinc-binding sites. These structures are discussed in comparison with those of the tetrameric L1 enzyme produced by Stenotrophomonas maltophilia. From this analysis, amino acids involved in the oligomerization of L1 are clearly identified. Despite the similarity in fold, the active site of FEZ-1 was found to be significantly different. Two residues, which were previously implicated in function, are not present in L1 or in FEZ-1. The broad-spectrum substrate profile of Zn-beta-lactamases arises from the rather wide active-site cleft, where various beta-lactam compounds can be accommodated.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
García-Sáez I,Mercuri PS,Papamicael C,Kahn R,Frère JM,Galleni M,Rossolini GM,Dideberg Odoi
10.1016/s0022-2836(02)01271-8keywords:
subject
Has Abstractpub_date
2003-01-24 00:00:00pages
651-60issue
4eissn
0022-2836issn
1089-8638pii
S0022283602012718journal_volume
325pub_type
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