1FOF

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10

Summary for 1FOF

• Entry DOI: 10.2210/pdb1fof/pdb
• Descriptor: BETA LACTAMASE OXA-10, COBALT (II) ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: beta-lactamase, class-d, oxacillinase, oxa-10, cobalt, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 55358.57

Authors

Paetzel, M.,Danel, F.,de Castro, L.,Mosimann, S.C.,Page, M.G.P.,Strynadka, N.C.J. (deposition date: 2000-08-28, release date: 2000-10-09, Last modification date: 2024-10-09)

Primary citation

Paetzel, M.,Danel, F.,de Castro, L.,Mosimann, S.C.,Page, M.G.,Strynadka, N.C.
Crystal structure of the class D beta-lactamase OXA-10.
Nat.Struct.Biol., 7:918-925, 2000

PubMed Abstract: We report the crystal structure of a class D beta-lactamase, the broad spectrum enzyme OXA-10 from Pseudomonas aeruginosa at 2.0 A resolution. There are significant differences between the overall fold observed in this structure and those of the evolutionarily related class A and class C beta-lactamases. Furthermore, the structure suggests the unique, cation mediated formation of a homodimer. Kinetic and hydrodynamic data shows that the dimer is a relevant species in solution and is the more active form of the enzyme. Comparison of the molecular details of the active sites of the class A and class C enzymes with the OXA-10 structure reveals that there is no counterpart in OXA-10 to the residues proposed to act as general bases in either of these enzymes (Glu 166 and Tyr 150, respectively). Our structures of the native and chloride inhibited forms of OXA-10 suggest that the class D enzymes have evolved a distinct catalytic mechanism for beta-lactam hydrolysis. Clinical variants of OXA-10 are also discussed in light of the structure.

PubMed: 11017203
DOI: 10.1038/79688

Experimental method

X-RAY DIFFRACTION (2 Å)