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1ye6
From Proteopedia
(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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| - | [[Image:1ye6.gif|left|200px]]<br /><applet load="1ye6" size=" | + | [[Image:1ye6.gif|left|200px]]<br /><applet load="1ye6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ye6, resolution 2.3Å" /> | caption="1ye6, resolution 2.3Å" /> | ||
'''Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+'''<br /> | '''Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aldo-keto reductases of family 2 employ single site replacement Lys-->Arg | + | 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== | ==About this Structure== | ||
| - | 1YE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tenuis Candida tenuis] with SO4, NAP and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tenuis Candida tenuis] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nidetzky, B.]] | [[Category: Nidetzky, B.]] | ||
[[Category: Petschacher, B.]] | [[Category: Petschacher, B.]] | ||
| - | [[Category: Wilson, D | + | [[Category: Wilson, D K.]] |
[[Category: NAD]] | [[Category: NAD]] | ||
[[Category: NAP]] | [[Category: NAP]] | ||
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[[Category: beta-alpha-barrel akr aldo-keto reductase coenzyme specificity nadp]] | [[Category: beta-alpha-barrel akr aldo-keto reductase coenzyme specificity nadp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:23 2008'' |
Revision as of 14:04, 21 February 2008
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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 , and 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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