1iyz

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[[Image:1iyz.gif|left|200px]]<br /><applet load="1iyz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1iyz.gif|left|200px]]
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caption="1iyz, resolution 2.80&Aring;" />
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'''Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH'''<br />
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{{Structure
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|PDB= 1iyz |SIZE=350|CAPTION= <scene name='initialview01'>1iyz</scene>, resolution 2.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5]
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|GENE=
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}}
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'''Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IYZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYZ OCA].
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1IYZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYZ OCA].
==Reference==
==Reference==
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Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition., Shimomura Y, Kakuta Y, Fukuyama K, J Bacteriol. 2003 Jul;185(14):4211-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837796 12837796]
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Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition., Shimomura Y, Kakuta Y, Fukuyama K, J Bacteriol. 2003 Jul;185(14):4211-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837796 12837796]
[[Category: NADPH:quinone reductase]]
[[Category: NADPH:quinone reductase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:56:48 2008''

Revision as of 09:56, 20 March 2008


PDB ID 1iyz

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Activity: NADPH:quinone reductase, with EC number 1.6.5.5
Coordinates: save as pdb, mmCIF, xml



Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH


Overview

The crystal structures of the zeta-crystalline-like soluble quinone oxidoreductase from Thermus thermophilus HB8 (QOR(Tt)) and of its complex with NADPH have been determined at 2.3- and 2.8-A resolutions, respectively. QOR(Tt) is composed of two domains, and its overall fold is similar to the folds of Escherichia coli quinone oxidoreductase (QOR(Ec)) and horse liver alcohol dehydrogenase. QOR(Tt) forms a homodimer in the crystal by interaction of the betaF-strands in domain II, forming a large beta-sheet that crosses the dimer interface. High thermostability of QOR(Tt) was evidenced by circular dichroic measurement. NADPH is located between the two domains in the QOR(Tt)-NADPH complex. The disordered segment involved in the coenzyme binding of apo-QOR(Tt) becomes ordered upon NADPH binding. The segment covers an NADPH-binding cleft and may serve as a lid. The 2'-phosphate group of the adenine of NADPH is surrounded by polar and positively charged residues in QOR(Tt), suggesting that QOR(Tt) binds NADPH more readily than NADH. The putative substrate-binding site of QOR(Tt), unlike that of QOR(Ec), is largely blocked by nearby residues, permitting access only to small substrates. This may explain why QOR(Tt) has weak p-benzoquinone reduction activity and is inactive with such large substrates of QOR(Ec) as 5-hydroxy-1,4-naphthoquinone and phenanthraquinone.

About this Structure

1IYZ is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition., Shimomura Y, Kakuta Y, Fukuyama K, J Bacteriol. 2003 Jul;185(14):4211-8. PMID:12837796

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