1ye6
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ye6.gif|left|200px]] | + | [[Image:1ye6.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+''' | + | {{Structure |
| + | |PDB= 1ye6 |SIZE=350|CAPTION= <scene name='initialview01'>1ye6</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= XYL1, XYLR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45596 Candida tenuis]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1YE6 is a [ | + | 1YE6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tenuis Candida tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE6 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15670843 15670843] |
[[Category: Candida tenuis]] | [[Category: Candida tenuis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:21:42 2008'' |
Revision as of 13:21, 20 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | XYL1, XYLR (Candida tenuis) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 15:21:42 2008
