1ye6
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(New page: 200px<br /><applet load="1ye6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ye6, resolution 2.3Å" /> '''Crystal structure of ...)
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Revision as of 04:35, 21 November 2007
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Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+
Overview
Aldo-keto reductases of family 2 employ single site replacement Lys-->Arg, to switch their cosubstrate preference from NADPH to NADH. X-ray crystal, structures of Lys-274-->Arg mutant of Candida tenuis xylose reductase, (AKR2B5) bound to NAD+ and NADP+ were determined at a resolution of 2.4, and 2.3A, respectively. Due to steric conflicts in the NADP+-bound form, the arginine side chain must rotate away from the position of the original, lysine side chain, thereby disrupting a network of direct and, water-mediated interactions between Glu-227, Lys-274 and the cofactor, 2'-phosphate and 3'-hydroxy groups. Because anchoring contacts of its, Glu-227 are lost, the coenzyme-enfolding loop that becomes ordered upon, binding of NAD(P)+ in the wild-type remains partly disordered in the, NADP+-bound mutant. The results delineate a catalytic reaction profile for, the mutant in comparison to wild-type.
About this Structure
1YE6 is a Single protein structure of sequence from Candida tenuis with SO4, NAP and NAD as ligands. Full crystallographic information is available from OCA.
Reference
Fine tuning of coenzyme specificity in family 2 aldo-keto reductases revealed by crystal structures of the Lys-274-->Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+ and NADP+., Leitgeb S, Petschacher B, Wilson DK, Nidetzky B, FEBS Lett. 2005 Jan 31;579(3):763-7. PMID:15670843
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