2z51

<StructureSection load='2z51' size='340' side='right' caption='[[2z51]], [[Resolution|resolution]] 1.35&Aring;' scene=''>

<table><tr><td colspan='2'>[[2z51]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z51 FirstGlance]. <br>

</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://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>

[[http://www.uniprot.org/uniprot/NIFU2_ARATH 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.<ref>PMID:15031412</ref> <ref>PMID:15361144</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z5/2z51_consurf.spt"</scriptWhenChecked>

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== 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<ref>PMID:18585737</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2z51" style="background-color:#fffaf0;"></div>

[[Category: Nakai, M]]

[[Category: Yabe, T]]

[[Category: Yamashita, E]]

[[Category: Cnfu]]

[[Category: Nif]]