2qr2
From Proteopedia
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| - | [[Image:2qr2.jpg|left|200px]] | + | [[Image:2qr2.jpg|left|200px]] |
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| - | '''HUMAN QUINONE REDUCTASE TYPE 2, COMPLEX WITH MENADIONE''' | + | {{Structure |
| + | |PDB= 2qr2 |SIZE=350|CAPTION= <scene name='initialview01'>2qr2</scene>, resolution 2.45Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=VK3:MENADIONE'>VK3</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN QUINONE REDUCTASE TYPE 2, COMPLEX WITH MENADIONE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QR2 is a [ | + | 2QR2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QR2 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of human quinone reductase type 2, a metalloflavoprotein., Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM, Biochemistry. 1999 Aug 3;38(31):9881-6. PMID:[http:// | + | Crystal structure of human quinone reductase type 2, a metalloflavoprotein., Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM, Biochemistry. 1999 Aug 3;38(31):9881-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10433694 10433694] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: NAD(P)H dehydrogenase (quinone)]] | [[Category: NAD(P)H dehydrogenase (quinone)]] | ||
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[[Category: quinone-reductase (cytosolic)]] | [[Category: quinone-reductase (cytosolic)]] | ||
| - | ''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 18:28:39 2008'' |
Revision as of 16:28, 20 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | NAD(P)H dehydrogenase (quinone), with EC number 1.6.5.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN QUINONE REDUCTASE TYPE 2, COMPLEX WITH MENADIONE
Overview
In mammals, two separate but homologous cytosolic quinone reductases have been identified: NAD(P)H:quinone oxidoreductase type 1 (QR1) (EC 1.6.99.2) and quinone reductase type 2 (QR2). Although QR1 and QR2 are nearly 50% identical in protein sequence, they display markedly different catalytic properties and substrate specificities. We report here two crystal structures of QR2: in its native form and bound to menadione (vitamin K(3)), a physiological substrate. Phases were obtained by molecular replacement, using our previously determined rat QR1 structure as the search model. QR2 shares the overall fold of the major catalytic domain of QR1, but lacks the smaller C-terminal domain. The FAD binding sites of QR1 and QR2 are very similar, but their hydride donor binding sites are considerably different. Unexpectedly, we found that QR2 contains a specific metal binding site, which is not present in QR1. Two histidine nitrogens, one cysteine thiol, and a main chain carbonyl group are involved in metal coordination. The metal binding site is solvent-accessible, and is separated from the FAD cofactor by a distance of about 13 A.
About this Structure
2QR2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human quinone reductase type 2, a metalloflavoprotein., Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM, Biochemistry. 1999 Aug 3;38(31):9881-6. PMID:10433694
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