1o94

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[[Image:1o94.jpg|left|200px]]
 
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{{Structure
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==Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein==
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|PDB= 1o94 |SIZE=350|CAPTION= <scene name='initialview01'>1o94</scene>, resolution 2.00&Aring;
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<StructureSection load='1o94' size='340' side='right'caption='[[1o94]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Sf4+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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<table><tr><td colspan='2'>[[1o94]] is a 6 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=1O94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O94 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trimethylamine_dehydrogenase Trimethylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.8.2 1.5.8.2] </span>
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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]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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|DOMAIN=
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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=1o94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o94 OCA], [https://pdbe.org/1o94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o94 RCSB], [https://www.ebi.ac.uk/pdbsum/1o94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o94 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o94 OCA], [http://www.ebi.ac.uk/pdbsum/1o94 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o94 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DHTM_METME DHTM_METME]
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== Evolutionary Conservation ==
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'''TERNARY COMPLEX BETWEEN TRIMETHYLAMINE DEHYDROGENASE AND ELECTRON TRANSFERRING FLAVOPROTEIN'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/1o94_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=1o94 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 ==
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.
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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==About this Structure==
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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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1O94 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=1O94 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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<div class="pdbe-citations 1o94" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[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: Trimethylamine dehydrogenase]]
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[[Category: Leys D]]
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[[Category: Basran, J.]]
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[[Category: Scrutton NS]]
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[[Category: Leys, D.]]
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[[Category: Sutcliffe MJ]]
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[[Category: Scrutton, N S.]]
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[[Category: Talfournier F]]
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[[Category: Sutcliffe, M J.]]
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[[Category: Talfournier, F.]]
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[[Category: dehydrogenase]]
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[[Category: electron transfer]]
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[[Category: protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:41:44 2008''
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Current revision

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

PDB ID 1o94

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