1ye4: Difference between revisions

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[[Image:1ye4.~~gif~~|left|200px]]

[[Image:1ye4.png|left|200px]]

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~~'''~~Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+~~'''~~

===Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_15670843}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15670843 is the PubMed ID number.

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==About this Structure==

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[[Category: Wilson, D K.]]

[[Category: Beta-alpha-barrel akr aldo-keto reductase coenzyme specificity nad]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 16~~:12:43 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:40:56 2008''

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-[[Image:1ye4.gif|left|200px]]
+{{Seed}}
+[[Image:1ye4.png|left|200px]]
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 {{STRUCTURE_1ye4|  PDB=1ye4  |  SCENE=  }}
-'''Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+'''
+===Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+===
-==Overview==
+<!--
-Aldo-keto reductases of family 2 employ single site replacement Lys--&gt;Arg to switch their cosubstrate preference from NADPH to NADH. X-ray crystal structures of Lys-274--&gt;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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15670843}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15670843 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15670843}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Wilson, D K.]]
 [[Category: Beta-alpha-barrel akr aldo-keto reductase coenzyme specificity nad]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:12:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:40:56 2008''