2v19
From Proteopedia
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| - | == | + | |
| - | <StructureSection load='2v19' size='340' side='right' caption='[[2v19]], [[Resolution|resolution]] 2.59Å' scene=''> | + | ==Crystal structure of the T. thermophilus dodecin R45A mutant== |
| + | <StructureSection load='2v19' size='340' side='right'caption='[[2v19]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2v19]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2v19]] 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=2V19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V19 FirstGlance]. <br> |
| - | </ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |
| - | <tr><td class="sblockLbl"><b> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v19 OCA], [https://pdbe.org/2v19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v19 RCSB], [https://www.ebi.ac.uk/pdbsum/2v19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v19 ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| + | [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> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/2v19_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/2v19_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> | ||
| - | </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/ | + | </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=2v19 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> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | <div class="pdbe-citations 2v19" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Thermus thermophilus]] | + | [[Category: Large Structures]] |
| - | [[Category: Essen | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Meissner | + | [[Category: Essen L-O]] |
| - | + | [[Category: Meissner B]] | |
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Current revision
Crystal structure of the T. thermophilus dodecin R45A mutant
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