1hf6
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(New page: 200px<br /> <applet load="1hf6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hf6, resolution 1.15Å" /> '''ENDOGLUCANASE CEL5A...)
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Revision as of 19:02, 29 October 2007
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ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE ORTHORHOMBIC CRYSTAL FORM IN COMPLEX WITH CELLOTRIOSE
Overview
Non-covalent interactions between protein and ligand at the active centre, of glycosidases play an enormous role in catalysis. Dissection of these, hydrogen-bonding networks is not merely important for an understanding of, enzymatic catalysis, but is also increasingly relevant for the design of, transition-state mimics, whose tautomeric state, hydrogen-bonding, interactions and protonation contribute to tight binding. Here, atomic, resolution ( approximately 1 A) analysis of a series of complexes of the, 34 kDa catalytic core domain of the Bacillus agaradhaerens endoglucanase, Cel5A is presented. Cel5A is a 'retaining' endoglucanase which performs, catalysis via the formation and subsequent breakdown of a covalent, glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states., ... [(full description)]
About this Structure
1HF6 is a [Single protein] structure of sequence from [Bacillus agaradhaerens] with SO4, CT3, ACY and GOL as [ligands]. Active as [[1]], with EC number [3.2.1.4]. Full crystallographic information is available from [OCA].
Reference
Direct experimental observation of the hydrogen-bonding network of a glycosidase along its reaction coordinate revealed by atomic resolution analyses of endoglucanase Cel5A., Varrot A, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):447-52. Epub 2003, Feb 21. PMID:12595701
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