PDBsum entry: 1l9y

Hydrolase

PDB id: 1l9y

Contents

Protein chains

263 a.a. *

Ligands

SO4 ×7

GOL ×4

Metals

_ZN ×4

_CL ×2

Waters ×319

* Residue conservation analysis

PDB id:

1l9y

Name:

Hydrolase

Title:

Fez-1-y228a, a mutant of the metallo-beta-lactamase from leg gormanii

Structure:

Fez-1 b-lactamase. Chain: a, b. Synonym: fez-1 protein. Engineered: yes. Mutation: yes

Source:

Fluoribacter gormanii. Organism_taxid: 464. Gene: blafez-1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.01Å R-factor: 0.186 R-free: 0.216

Authors:

I.Garcia-Saez,P.S.Mercuri,M.Galleni,O.Dideberg

Key ref:

I.García-Sáez et al. (2003). Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril. J Mol Biol, 325, 651-660. PubMed id: 12507470 DOI: 10.1016/S0022-2836(02)01271-8

Date:

27-Mar-02 Release date: 01-Jul-03

Protein chains

Q9K578  (Q9K578_9GAMM) -  FEZ-1 protein

Seq: 282 a.a.

Struc: 263 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biochemical function: hydrolase activity (2 terms)

DOI no: 10.1016/S0022-2836(02)01271-8

J Mol Biol 325:651-660 (2003)

PubMed id: 12507470

Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril.

I.García-Sáez, P.S.Mercuri, C.Papamicael, R.Kahn, J.M.Frère, M.Galleni, G.M.Rossolini, O.Dideberg.

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.

Selected figure(s)

Figure 3.
Figure 3. A representation of Ser221 and Wat127/178, close to the active site of native FEZ-1. The alternate conformation of Ser221 with occupancy 0.3 due to a rotation of 103.98 of its hydroxyl group from the main conformation (blue) is depicted in pink. In that main position, Ser221 is hydrogen bonding Wat127/178. In the second conformation, the water is released by Ser221 and attracted close to the Zn ions. The Figure was made using TURBO.

The above figure is reprinted by permission from Elsevier: J Mol Biol (2003, 325, 651-660) copyright 2003.

Figure was selected by an automated process.