2QZ6

First crystal structure of a psychrophile class C beta-lactamase

Summary for 2QZ6

• Entry DOI: 10.2210/pdb2qz6/pdb
• Descriptor: Beta-lactamase (2 entities in total)
• Functional Keywords: class c beta-lactamase, psychrophile, cold adaptation, antibiotic resistance, hydrolase, periplasm
• Biological source: Pseudomonas fluorescens
• Cellular location: Periplasm: P85302
• Total number of polymer chains: 1
• Total formula weight: 38764.91

Authors

Michaux, C.,Massant, J.,Kerff, F.,Charlier, P.,Wouters, J. (deposition date: 2007-08-16, release date: 2008-03-18, Last modification date: 2023-10-25)

Primary citation

Michaux, C.,Massant, J.,Kerff, F.,Docquier, J.D.,Vandenberghe, I.,Samyn, B.,Pierrard, A.,Feller, G.,Charlier, P.,Van Beeumen, J.,Wouters, J.
Crystal structure of a cold-adapted class C beta-lactamase
Febs J., 275:1687-1697, 2008

PubMed Abstract: In this study, the crystal structure of a class C beta-lactamase from a psychrophilic organism, Pseudomonas fluorescens, has been refined to 2.2 A resolution. It is one of the few solved crystal structures of psychrophilic proteins. The structure was compared with those of homologous mesophilic enzymes and of another, modeled, psychrophilic protein. The elucidation of the 3D structure of this enzyme provides additional insights into the features involved in cold adaptation. Structure comparison of the psychrophilic and mesophilic beta-lactamases shows that electrostatics seems to play a major role in low-temperature adaptation, with a lower total number of ionic interactions for cold enzymes. The psychrophilic enzymes are also characterized by a decreased number of hydrogen bonds, a lower content of prolines, and a lower percentage of arginines in comparison with lysines. All these features make the structure more flexible so that the enzyme can behave as an efficient catalyst at low temperatures.

PubMed: 18312599
DOI: 10.1111/j.1742-4658.2008.06324.x

Experimental method

X-RAY DIFFRACTION (2.26 Å)