1ye6
From Proteopedia
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|PDB= 1ye6 |SIZE=350|CAPTION= <scene name='initialview01'>1ye6</scene>, resolution 2.3Å | |PDB= 1ye6 |SIZE=350|CAPTION= <scene name='initialview01'>1ye6</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= XYL1, XYLR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45596 Candida tenuis]) | |GENE= XYL1, XYLR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45596 Candida tenuis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ye4|1YE4]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ye6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ye6 OCA], [http://www.ebi.ac.uk/pdbsum/1ye6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ye6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Petschacher, B.]] | [[Category: Petschacher, B.]] | ||
[[Category: Wilson, D K.]] | [[Category: Wilson, D K.]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: NAP]] | ||
| - | [[Category: SO4]] | ||
[[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://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:04:27 2008'' |
Revision as of 22:04, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | XYL1, XYLR (Candida tenuis) | ||||||
| Related: | 1YE4
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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