1pr9
From Proteopedia
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|PDB= 1pr9 |SIZE=350|CAPTION= <scene name='initialview01'>1pr9</scene>, resolution 1.96Å | |PDB= 1pr9 |SIZE=350|CAPTION= <scene name='initialview01'>1pr9</scene>, resolution 1.96Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/L-xylulose_reductase L-xylulose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.10 1.1.1.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-xylulose_reductase L-xylulose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.10 1.1.1.10] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pr9 OCA], [http://www.ebi.ac.uk/pdbsum/1pr9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pr9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ishikura, S.]] | [[Category: Ishikura, S.]] | ||
[[Category: Usami, N.]] | [[Category: Usami, N.]] | ||
| - | [[Category: 2HP]] | ||
| - | [[Category: K]] | ||
| - | [[Category: NAP]] | ||
[[Category: dinucleotide binding domain]] | [[Category: dinucleotide binding domain]] | ||
[[Category: short chain dehydrogenase/reductase]] | [[Category: short chain dehydrogenase/reductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:03:27 2008'' |
Revision as of 20:03, 30 March 2008
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| , resolution 1.96Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | L-xylulose reductase, with EC number 1.1.1.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Human L-Xylulose Reductase Holoenzyme
Overview
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 (>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.
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
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