1ye4

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[[Image:1ye4.gif|left|200px]]
[[Image:1ye4.gif|left|200px]]
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{{Structure
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|PDB= 1ye4 |SIZE=350|CAPTION= <scene name='initialview01'>1ye4</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1ye4", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|GENE= XYL1, XYLR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45596 Candida tenuis])
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|DOMAIN=
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{{STRUCTURE_1ye4| PDB=1ye4 | SCENE= }}
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|RELATEDENTRY=[[1ye6|1YE6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ye4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ye4 OCA], [http://www.ebi.ac.uk/pdbsum/1ye4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ye4 RCSB]</span>
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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+'''
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[[Category: Petschacher, B.]]
[[Category: Petschacher, B.]]
[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
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[[Category: beta-alpha-barrel akr aldo-keto reductase coenzyme specificity nad]]
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[[Category: Beta-alpha-barrel akr aldo-keto reductase coenzyme specificity nad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:12:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:04:27 2008''
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Revision as of 13:12, 3 May 2008

Image:1ye4.gif

Template:STRUCTURE 1ye4

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-->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

1YE4 is a Single protein structure of sequence from Candida tenuis. 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 Page seeded by OCA on Sat May 3 16:12:43 2008

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