Crystal structure of the class D beta-lactamase OXA-10

Autor:	M, Paetzel, F, Danel, L, de Castro, S C, Mosimann, M G, Page, N C, Strynadka
Rok vydání:	2000
Předmět:	Models Molecular Protein Folding Binding Sites Sequence Homology Amino Acid Molecular Sequence Data Point Mutation Amino Acid Sequence Dimerization beta-Lactamases
Zdroj:	Nature structural biology. 7(10)
ISSN:	1072-8368
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::a810ffcc8eb417e6232324bdbfa9b495 https://pubmed.ncbi.nlm.nih.gov/11017203 Zobrazit plný text záznamu Full text from SpringerLink