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2vkr

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Revision as of 10:46, 7 July 2021

3Fe-4S, 4Fe-4S plus Zn Acidianus ambivalens ferredoxin

Structural highlights

2vkr is a 7 chain structure with sequence from Acidianus ambivalens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Detailed 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.

References

↑ Frazao C, Aragao D, Coelho R, Leal SS, Gomes CM, Teixeira M, Carrondo MA. Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+) -containing ferredoxin. FEBS Lett. 2008 Mar 5;582(5):763-7. Epub 2008 Feb 5. PMID:18258200 doi:http://dx.doi.org/10.1016/j.febslet.2008.01.041

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vkr"

@@ Line 3: / Line 3: @@
 <StructureSection load='2vkr' size='340' side='right'caption='[[2vkr]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
 == Structural highlights ==
-<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 [https://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 [https://proteopedia.org/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" id="ligandDat"><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://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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkr OCA], [https://pdbe.org/2vkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vkr RCSB], [https://www.ebi.ac.uk/pdbsum/2vkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vkr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FER_ACIAM 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.
+[[https://www.uniprot.org/uniprot/FER_ACIAM 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Ferredoxin|Ferredoxin]]
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 == References ==
 <references/>

2vkr

From Proteopedia

Revision as of 10:46, 7 July 2021

3Fe-4S, 4Fe-4S plus Zn Acidianus ambivalens ferredoxin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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