Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537551 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2014 | 9 Pages |
Abstract
The crystallographic structure of the homooctameric Rho-2-CMCI was solved by molecular replacement using the coordinates of the structure of chloromuconate cycloisomerase from Pseudomonas putida PRS2000. The structure was analyzed and compared to the other already known structures of (chloro)muconate cycloisomerases. In addition to this, molecular docking calculations were carried out, which allowed us to determine the residues responsible for the high substrate specificity and the lack of dehalogenation activity of Rho-2-CMCI. Our studies highlight that a histidine, located in a loop that closes the active site cavity upon the binding of the substrate, could be related to the dehalogenation inability of Rho-2-CMCI and in general of the muconate cycloisomerases.
Related Topics
Physical Sciences and Engineering
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Analytical Chemistry
Authors
Marina Kolomytseva, Marta Ferraroni, Alexey Chernykh, Ludmila Golovleva, Andrea Scozzafava,