1pr9

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{{STRUCTURE_1pr9| PDB=1pr9 | SCENE= }}
{{STRUCTURE_1pr9| PDB=1pr9 | SCENE= }}
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'''Human L-Xylulose Reductase Holoenzyme'''
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===Human L-Xylulose Reductase Holoenzyme===
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==Overview==
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L-Xylulose reductase (XR), an enzyme in the uronate cycle of glucose metabolism, belongs to the short-chain dehydrogenase/reductase (SDR) superfamily. Among the SDR enzymes, XR shows the highest sequence identity (67%) with mouse lung carbonyl reductase (MLCR), but the two enzymes show different substrate specificities. The crystal structure of human XR in complex with reduced nicotinamide adenine dinucleotide phosphate (NADPH) was determined at 1.96 A resolution by using the molecular replacement method and the structure of MLCR as the search model. Features unique to human XR include electrostatic interactions between the N-terminal residues of subunits related by the P-axis, termed according to SDR convention, and an interaction between the hydroxy group of Ser185 and the pyrophosphate of NADPH. Furthermore, identification of the residues lining the active site of XR (Cys138, Val143, His146, Trp191, and Met200) together with a model structure of XR in complex with L-xylulose, revealed structural differences with other members of the SDR family, which may account for the distinct substrate specificity of XR. The residues comprising a recently proposed catalytic tetrad in the SDR enzymes are conserved in human XR (Asn107, Ser136, Tyr149, and Lys153). To examine the role of Asn107 in the catalytic mechanism of human XR, mutant forms (N107D and N107L) were prepared. The two mutations increased K(m) for the substrate (&gt;26-fold) and K(d) for NADPH (95-fold), but only the N107L mutation significantly decreased k(cat) value. These results suggest that Asn107 plays a critical role in coenzyme binding rather than in the catalytic mechanism.
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(as it appears on PubMed at http://www.pubmed.gov), where 15103634 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15103634}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis., El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A, Proteins. 2004 May 15;55(3):724-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103634 15103634]
Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis., El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A, Proteins. 2004 May 15;55(3):724-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103634 15103634]
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Crystallization and preliminary crystallographic analysis of human L-xylulose reductase., El-Kabbani O, Chung RP, Ishikura S, Usami N, Nakagawa J, Hara A, Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1379-80. Epub 2002, Jul 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12136162 12136162]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: L-xylulose reductase]]
[[Category: L-xylulose reductase]]
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[[Category: Dinucleotide binding domain]]
[[Category: Dinucleotide binding domain]]
[[Category: Short chain dehydrogenase/reductase]]
[[Category: Short chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:23:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:05:28 2008''

Revision as of 00:05, 29 July 2008

Image:1pr9.png

Template:STRUCTURE 1pr9

Human L-Xylulose Reductase Holoenzyme

Template:ABSTRACT PUBMED 15103634

About this Structure

1PR9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis., El-Kabbani O, Ishikura S, Darmanin C, Carbone V, Chung RP, Usami N, Hara A, Proteins. 2004 May 15;55(3):724-32. PMID:15103634

Crystallization and preliminary crystallographic analysis of human L-xylulose reductase., El-Kabbani O, Chung RP, Ishikura S, Usami N, Nakagawa J, Hara A, Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1379-80. Epub 2002, Jul 20. PMID:12136162

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