2qwx: Difference between revisions

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==Crystal Structure of Quinone Reductase II==
The line below this paragraph, containing "STRUCTURE_2qwx", creates the "Structure Box" on the page.
<StructureSection load='2qwx' size='340' side='right'caption='[[2qwx]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2qwx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QWX FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=ML1:N-[2-(5-METHOXY-1H-INDOL-3-YL)ETHYL]ACETAMIDE'>ML1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2qwx| PDB=2qwx |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qwx OCA], [https://pdbe.org/2qwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qwx RCSB], [https://www.ebi.ac.uk/pdbsum/2qwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qwx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/2qwx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qwx ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of Quinone Reductase II'''
==See Also==
 
*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
 
== References ==
==Overview==
<references/>
Melatonin exerts its biological effects through at least two transmembrane, G-coupled receptors, MT1 and MT2, and a lower affinity, cytosolic binding site, designated MT3. MT3 has recently been identified as quinone reductase 2 (QR2, E.C. 1.10.99.2) which is of significance since it links the anti-oxidant effects of melatonin to a mechanism-of-action. Initially, QR2 was believed to function analogously to QR1 in protecting cells from highly reactive quinones. However, recent studies indicate that QR2 may actually transform certain quinone substrates into more highly reactive compounds capable of causing cellular damage. Therefore, it is hypothesized that inhibition of QR2 in certain causes may lead to protection of cells against these highly reactive species. Since melatonin is known to inhibit QR2 activity, but its binding site and mode of inhibition are not known, we determined the mechanism of inhibition of QR2 by melatonin and a series of melatonin and serotonin analogs, and we determined the x-ray structures of melatonin and 2-iodomelatonin in complex with QR2 to between 1.5 and 1.8 A resolution. Finally, the thermodynamic binding constants for melatonin and 2-iodomelatonin were determined by isothermal titration calorimetry (ITC). The kinetic results indicate that melatonin is a competitive inhibitor against N-methyldihydronicotinamide (Ki = 7.2 microM) and uncompetitive against menadione (Ki = 92 microM), and the x-ray structures shows that melatonin binds in multiple orientations within the active sites of the QR2 dimer as opposed to an allosteric site. These results provide new insights into the binding mechanisms of melatonin and analogs to QR2.
__TOC__
 
</StructureSection>
==About this Structure==
2QWX 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=2QWX OCA].
 
==Reference==
Kinetic, thermodynamic, and X-ray structural insights into the interaction of melatonin and analogs with quinone reductase 2., Calamini B, Santarsiero BD, Boutin JA, Mesecar AD, Biochem J. 2008 Feb 7;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18254726 18254726]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Boutin, J A.]]
[[Category: Boutin JA]]
[[Category: Calamini, B.]]
[[Category: Calamini B]]
[[Category: Mesecar, A D.]]
[[Category: Mesecar AD]]
[[Category: Santarsiero, B D.]]
[[Category: Santarsiero BD]]
[[Category: Cytoplasm]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Metal-binding]]
[[Category: Oxidoreductase]]
[[Category: Polymorphism]]
[[Category: Qr2]]
[[Category: Zinc]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:18:09 2008''

Latest revision as of 12:18, 21 February 2024

Crystal Structure of Quinone Reductase IICrystal Structure of Quinone Reductase II

Structural highlights

2qwx is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NQO2_HUMAN The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Calamini B, Santarsiero BD, Boutin JA, Mesecar AD. Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2. Biochem J. 2008 Jul 1;413(1):81-91. PMID:18254726 doi:10.1042/BJ20071373

2qwx, resolution 1.50Å

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