1ozk

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1ozk.png|left|200px]]
 
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==THEORETICAL MODEL FOR NADH-UBIQUINONE REDUCTASE==
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The line below this paragraph, containing "STRUCTURE_1ozk", creates the "Structure Box" on the page.
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<StructureSection load='1ozk' size='340' side='right'caption='[[1ozk]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OZK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ozk FirstGlance], [https://www.ebi.ac.uk/pdbsum/1ozk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozk ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1ozk| PDB=1ozk | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The alternative NADH:ubiquinone oxidoreductase (NDH-2) from Escherichia coli is a membrane protein playing a prominent role in respiration by linking the reduction of NADH to the quinone pool. Remote sequence similarity reveals an evolutionary relation between alternative NADH:quinone oxidoreductases and the SCOP-family "FAD/NAD-linked reductases". We have created a structural model for NDH-2 from E. coli through comparative modelling onto a template from this family. Combined analysis of our model and sequence conservation allowed us to include the cofactor FAD and the substrate NADH in atomic detail. Furthermore, we propose the most plausible orientation of NDH-2 relative to the membrane and specify a region of the protein potentially involved in ubiquinone binding.
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===THEORETICAL MODEL FOR NADH-UBIQUINONE REDUCTASE===
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Functional properties of the alternative NADH:ubiquinone oxidoreductase from E. coli through comparative 3-D modelling.,Schmid R, Gerloff DL FEBS Lett. 2004 Dec 3;578(1-2):163-8. PMID:15581635<ref>PMID:15581635</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15581635}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ozk" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15581635 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15581635}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZK OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:15581635</ref><references group="xtra"/>
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[[Category: Gerloff, D L]]
[[Category: Gerloff, D L]]
[[Category: Schmid, R]]
[[Category: Schmid, R]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:10:05 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THEORETICAL MODEL FOR NADH-UBIQUINONE REDUCTASE

PDB ID 1ozk

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