1iyz: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="1iyz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iyz, resolution 2.80Å" /> '''Crystal Structures o... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1iyz.gif|left|200px]]<br /><applet load="1iyz" size=" | [[Image:1iyz.gif|left|200px]]<br /><applet load="1iyz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1iyz, resolution 2.80Å" /> | caption="1iyz, resolution 2.80Å" /> | ||
'''Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH'''<br /> | '''Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structures of the zeta-crystalline-like soluble quinone | 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== | ==About this Structure== | ||
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 NDP 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:// | 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]. | ||
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Fukuyama, K.]] | [[Category: Fukuyama, K.]] | ||
[[Category: Kakuta, Y.]] | [[Category: Kakuta, Y.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Shimomura, Y.]] | [[Category: Shimomura, Y.]] | ||
[[Category: NDP]] | [[Category: NDP]] | ||
| Line 24: | Line 24: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:10 2008'' | ||
