6rxn
From Proteopedia
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| - | [[Image:6rxn.gif|left|200px]]<br /><applet load="6rxn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="6rxn, resolution 1.5Å" /> | ||
| - | '''THE STRUCTURE OF RUBREDOXIN FROM DESULFOVIBRIO DESULFURICANS'''<br /> | ||
| - | == | + | ==THE STRUCTURE OF RUBREDOXIN FROM DESULFOVIBRIO DESULFURICANS== |
| + | <StructureSection load='6rxn' size='340' side='right'caption='[[6rxn]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RXN 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]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene></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=6rxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rxn OCA], [https://pdbe.org/6rxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rxn RCSB], [https://www.ebi.ac.uk/pdbsum/6rxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rxn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RUBR1_DESDA RUBR1_DESDA] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Electron acceptor for cytoplasmic lactate dehydrogenase. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/6rxn_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=6rxn ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The structure of a small rubredoxin from the bacterium Desulfovibrio desulfuricans has been determined and refined at 1.5 A resolution. The hairpin loop containing seven residues in other rubredoxins is missing in this 45 residue molecule, and once that fact was determined by amino acid sequencing studies, refinement progressed smoothly to an R value of 0.093 for all reflections from 5 to 1.5 A resolution. Nearly all of the water molecules in the well-ordered triclinic unit cell have been added to the crystallographic model. As in the other refined rubredoxin models, the Fe-S4 complex is slightly distorted from ideal tetrahedral coordination. | The structure of a small rubredoxin from the bacterium Desulfovibrio desulfuricans has been determined and refined at 1.5 A resolution. The hairpin loop containing seven residues in other rubredoxins is missing in this 45 residue molecule, and once that fact was determined by amino acid sequencing studies, refinement progressed smoothly to an R value of 0.093 for all reflections from 5 to 1.5 A resolution. Nearly all of the water molecules in the well-ordered triclinic unit cell have been added to the crystallographic model. As in the other refined rubredoxin models, the Fe-S4 complex is slightly distorted from ideal tetrahedral coordination. | ||
| - | + | The structure of rubredoxin from Desulfovibrio desulfuricans strain 27774 at 1.5 A resolution.,Stenkamp RE, Sieker LC, Jensen LH Proteins. 1990;8(4):352-64. PMID:2091025<ref>PMID:2091025</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6rxn" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Rubredoxin 3D structures|Rubredoxin 3D structures]] | ||
| + | *[[Rubredoxin PDB structures|Rubredoxin PDB structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Desulfovibrio desulfuricans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jensen LH]] | ||
| + | [[Category: Sieker LC]] | ||
| + | [[Category: Stenkamp RE]] | ||
Current revision
THE STRUCTURE OF RUBREDOXIN FROM DESULFOVIBRIO DESULFURICANS
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