2BMI

METALLO-BETA-LACTAMASE

Replaces:  1BMI

Summary for 2BMI

• Entry DOI: 10.2210/pdb2bmi/pdb
• Descriptor: PROTEIN (CLASS B BETA-LACTAMASE), ZINC ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: beta-lactamase, metallo beta-lactamase, zinc, hydrolase
• Biological source: Bacteroides fragilis
• Total number of polymer chains: 2
• Total formula weight: 51024.87

Authors

Carfi, A.,Duee, E.,Dideberg, O. (deposition date: 1998-09-17, release date: 1998-09-23, Last modification date: 2024-02-14)

Primary citation

Carfi, A.,Duee, E.,Paul-Soto, R.,Galleni, M.,Frere, J.M.,Dideberg, O.
X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
Acta Crystallogr.,Sect.D, 54:45-57, 1998

PubMed Abstract: beta-Lactamases are extracellular or periplasmic bacterial enzymes which confer resistance to beta-lactam antibiotics. On the basis of their catalytic mechanisms, they can be divided into two major groups: active-site serine enzymes (classes A, C and D) and the ZnII enzymes (class B). The first crystal structure of a class B enzyme, the metallo-beta-lactamase from Bacillus cereus, has been solved at 2.5 A resolution [Carfi, Pares, Duée, Galleni, Duez, Frère & Dideberg (1995). EMBO J. 14, 4914-4921]. Recently, the crystal structure of the metallo-beta-lactamase from Bacteroides fragilis has been determined in a tetragonal space group [Concha, Rasmussen, Bush & Herzberg (1996). Structure, 4, 823-836]. The structure of the metallo-beta-lactamase from B. fragilis in an orthorhombic crystal form at 2.0 A resolution is reported here. The final crystallographic R is 0.196 for all the 32501 observed reflections in the range 10-2.0 A. The refined model includes 458 residues, 437 water molecules, four zinc and two sodium ions. These structures are discussed with reference to Zn binding and activity. A catalytic mechanism is proposed which is coherent with metallo-beta-lactamases being active with either one Zn ion (as in Aeromonas hydrophila) or two Zn ions (as in B. fragilis) bound to the protein.

PubMed: 9761816
DOI: 10.1107/S090744499700927X

Experimental method

X-RAY DIFFRACTION (2 Å)