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2z51

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Revision as of 12:23, 7 February 2016

Crystal structure of Arabidopsis CnfU involved in iron-sulfur cluster biosynthesis

Structural highlights

2z51 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	NIFU2, CNFU2, NFU2 (Arabidopsis thaliana)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[NIFU2_ARATH] Molecular scaffold for [Fe-S] cluster assembly of chloroplastic iron-sulfur proteins. Required for biogenesis of ferredoxin, a major photosynthetic electron carrier containing [2Fe-2S] cluster. Required for the assembly of photosystem I complex.^[1] ^[2]

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

CnfU, a key iron-sulfur (Fe-S) cluster biosynthetic scaffold that is required for biogenesis of ferredoxin and photosystem I in chloroplasts, consists of two tandemly repeated domains in which only the N-terminal domain contains a conserved CXXC motif. We have determined the crystal structure of the metal-free dimer of AtCnfU-V from Arabidopsis thaliana at 1.35 A resolution. The N-terminal domains of the two monomers are linked together through two intermolecular disulfide bonds between the CXXC motifs. At the dimer interface, a total of four cysteine sulfur atoms provide a Fe-S cluster assembly site surrounded by uncharged but hydrophilic structurally mobile segments. The C-terminal domain of one monomer interacts with the N-terminal domain of the opposing monomer and thereby stabilizes dimer formation. Furthermore, Fe K-edge X-ray absorption spectroscopic analysis of the holo-CnfU dimer in solution suggests the presence of a typical [2Fe-2S]-type cluster coordinated by four thiolate ligands. Based on these data, a plausible model of the holo-AtCnfU-V dimer containing a surface-exposed [2Fe-2S] cluster assembled in the dimer interface was deduced. We propose that such a structural framework is important for CnfU to function as a Fe-S cluster biosynthetic scaffold.

Structural analysis of Arabidopsis CnfU protein: an iron-sulfur cluster biosynthetic scaffold in chloroplasts.,Yabe T, Yamashita E, Kikuchi A, Morimoto K, Nakagawa A, Tsukihara T, Nakai M J Mol Biol. 2008 Aug 1;381(1):160-73. Epub 2008 Jun 4. PMID:18585737^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yabe T, Morimoto K, Kikuchi S, Nishio K, Terashima I, Nakai M. The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an iron-sulfur cluster scaffold protein, is required for biogenesis of ferredoxin and photosystem I. Plant Cell. 2004 Apr;16(4):993-1007. Epub 2004 Mar 18. PMID:15031412 doi:http://dx.doi.org/10.1105/tpc.020511
↑ Touraine B, Boutin JP, Marion-Poll A, Briat JF, Peltier G, Lobreaux S. Nfu2: a scaffold protein required for [4Fe-4S] and ferredoxin iron-sulphur cluster assembly in Arabidopsis chloroplasts. Plant J. 2004 Oct;40(1):101-11. PMID:15361144 doi:http://dx.doi.org/10.1111/j.1365-313X.2004.02189.x
↑ Yabe T, Yamashita E, Kikuchi A, Morimoto K, Nakagawa A, Tsukihara T, Nakai M. Structural analysis of Arabidopsis CnfU protein: an iron-sulfur cluster biosynthetic scaffold in chloroplasts. J Mol Biol. 2008 Aug 1;381(1):160-73. Epub 2008 Jun 4. PMID:18585737 doi:10.1016/j.jmb.2008.05.072

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z51"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NIFU2, CNFU2, NFU2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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=2z51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z51 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z51 RCSB], [http://www.ebi.ac.uk/pdbsum/2z51 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=2z51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z51 OCA], [http://pdbe.org/2z51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z51 RCSB], [http://www.ebi.ac.uk/pdbsum/2z51 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2z51 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2z51" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2z51

From Proteopedia

Revision as of 12:23, 7 February 2016

Crystal structure of Arabidopsis CnfU involved in iron-sulfur cluster biosynthesis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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