2qz6
From Proteopedia
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| , resolution 2.26Å | |||||||
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| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
First crystal structure of a psychrophile class C beta-lactamase
Overview
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.
About this Structure
2QZ6 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a cold-adapted class C beta-lactamase., Michaux C, Massant J, Kerff F, Frere JM, Docquier JD, Vandenberghe I, Samyn B, Pierrard A, Feller G, Charlier P, Van Beeumen J, Wouters J, FEBS J. 2008 Feb 29;. PMID:18312599
Page seeded by OCA on Thu Mar 20 18:31:05 2008
