1o97

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{{Seed}}
 
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[[Image:1o97.png|left|200px]]
 
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==Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis==
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The line below this paragraph, containing "STRUCTURE_1o97", creates the "Structure Box" on the page.
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<StructureSection load='1o97' size='340' side='right'caption='[[1o97]], [[Resolution|resolution]] 1.60&Aring;' 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'>[[1o97]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O97 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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{{STRUCTURE_1o97| PDB=1o97 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o97 OCA], [https://pdbe.org/1o97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o97 RCSB], [https://www.ebi.ac.uk/pdbsum/1o97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o97 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ETFB_METME ETFB_METME] The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/1o97_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1o97 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Here we report the crystal structures of a ternary electron transfer complex showing extensive motion at the protein interface. This physiological complex comprises the iron-sulfur flavoprotein trimethylamine dehydrogenase and electron transferring flavoprotein (ETF) from Methylophilus methylotrophus. In addition, we report the crystal structure of free ETF. In the complex, electron density for the FAD domain of ETF is absent, indicating high mobility. Positions for the FAD domain are revealed by molecular dynamics simulation, consistent with crystal structures and kinetic data. A dual interaction of ETF with trimethylamine dehydrogenase provides for dynamical motion at the protein interface: one site acts as an anchor, thereby allowing the other site to sample a large range of interactions, some compatible with rapid electron transfer. This study establishes the role of conformational sampling in multi-domain redox systems, providing insight into electron transfer between ETFs and structurally distinct redox partners.
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===STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPHUS, RECOGNITION LOOP REMOVED BY LIMITED PROTEOLYSIS===
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Extensive conformational sampling in a ternary electron transfer complex.,Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:12567183<ref>PMID:12567183</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_12567183}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1o97" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12567183 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12567183}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1O97 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O97 OCA].
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==Reference==
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Extensive conformational sampling in a ternary electron transfer complex., Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS, Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12567183 12567183]
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[[Category: Methylophilus methylotrophus]]
[[Category: Methylophilus methylotrophus]]
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[[Category: Protein complex]]
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[[Category: Basran J]]
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[[Category: Basran, J.]]
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[[Category: Leys D]]
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[[Category: Leys, D.]]
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[[Category: Scrutton NS]]
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[[Category: Scrutton, N S.]]
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[[Category: Sutcliffe MJ]]
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[[Category: Sutcliffe, M J.]]
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[[Category: Talfournier F]]
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[[Category: Talfournier, F.]]
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[[Category: Electron transfer]]
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[[Category: Fad binding]]
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[[Category: Flavoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:48:55 2008''
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Current revision

Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis

PDB ID 1o97

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