2v18

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==CRYSTAL STRUCTURE OF THE T. THERMOPHILUS DODECIN==
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<StructureSection load='2v18' size='340' side='right' caption='[[2v18]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
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==Crystal structure of the T. thermophilus dodecin==
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<StructureSection load='2v18' size='340' side='right'caption='[[2v18]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2v18]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V18 OCA]. <br>
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<table><tr><td colspan='2'>[[2v18]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V18 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><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]] 2.59&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ux9|2ux9]], [[2v19|2v19]], [[2v21|2v21]]</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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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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=2v18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v18 OCA], [https://pdbe.org/2v18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v18 RCSB], [https://www.ebi.ac.uk/pdbsum/2v18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v18 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v18 RCSB], [http://www.ebi.ac.uk/pdbsum/2v18 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/DODEC_THET8 DODEC_THET8] May function as storage protein that sequesters various flavins and other cofactors, thereby protecting the cell against undesirable reactions mediated by the free cofactors. Binds and sequesters FMN, FAD, lumiflavin and lumichrome, and can also bind coenzyme A.<ref>PMID:17855371</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/2v18_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/2v18_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2v18 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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The dodecin from Thermus thermophilus, a bifunctional cofactor storage protein.,Meissner B, Schleicher E, Weber S, Essen LO J Biol Chem. 2007 Nov 9;282(45):33142-54. Epub 2007 Sep 11. PMID:17855371<ref>PMID:17855371</ref>
The dodecin from Thermus thermophilus, a bifunctional cofactor storage protein.,Meissner B, Schleicher E, Weber S, Essen LO J Biol Chem. 2007 Nov 9;282(45):33142-54. Epub 2007 Sep 11. PMID:17855371<ref>PMID:17855371</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2v18" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Thermus thermophilus]]
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[[Category: Large Structures]]
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[[Category: Essen, L O.]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Meissner, B.]]
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[[Category: Essen L-O]]
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[[Category: Coenzyme some]]
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[[Category: Meissner B]]
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[[Category: Dodecin]]
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[[Category: Flavin binding protein]]
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[[Category: Flavin dimer]]
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[[Category: Flavoprotein]]
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[[Category: Flavoprotein putative storage protein]]
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[[Category: Hypothetical protein]]
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Current revision

Crystal structure of the T. thermophilus dodecin

PDB ID 2v18

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