2vkr: Difference between revisions
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==3FE-4S, 4FE-4S PLUS ZN ACIDIANUS AMBIVALENS FERREDOXIN== | ==3FE-4S, 4FE-4S PLUS ZN ACIDIANUS AMBIVALENS FERREDOXIN== | ||
<StructureSection load='2vkr' size='340' side='right' caption='[[2vkr]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='2vkr' size='340' side='right' caption='[[2vkr]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
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<table><tr><td colspan='2'>[[2vkr]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vkr]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vkr RCSB], [http://www.ebi.ac.uk/pdbsum/2vkr PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkr OCA], [http://pdbe.org/2vkr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkr RCSB], [http://www.ebi.ac.uk/pdbsum/2vkr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<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=2vkr 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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2vkr" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 08:19, 5 August 2016
3FE-4S, 4FE-4S PLUS ZN ACIDIANUS AMBIVALENS FERREDOXIN3FE-4S, 4FE-4S PLUS ZN ACIDIANUS AMBIVALENS FERREDOXIN
Structural highlights
Function[FER_ACIAM] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. The 3Fe-4S cluster is reduced by a flavoprotein with NADH oxidase activity from the same organism. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDetailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 A resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn(2+) site and the ferredoxin (betaalphabeta)(2) core, which harbours intact clusters I and II, a [3Fe-4S](1+/0) and a [4Fe-4S](2+/1+) centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S](1+/0) centres and poor definition around cluster II. Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+) -containing ferredoxin.,Frazao C, Aragao D, Coelho R, Leal SS, Gomes CM, Teixeira M, Carrondo MA FEBS Lett. 2008 Mar 5;582(5):763-7. Epub 2008 Feb 5. PMID:18258200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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