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3tbn

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Crystal structure of a miner2 homolog: a type 6 CDGSH iron-sulfur protein.

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Retrieved from "http://52.214.119.220/wiki/index.php/3tbn"

Categories: Large Structures | Magnetospirillum magneticum AMB-1 | Lin J | Ye K | Zhang L

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 <StructureSection load='3tbn' size='340' side='right'caption='[[3tbn]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tbn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Magsa Magsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TBN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tbn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospirillum_magneticum_AMB-1 Magnetospirillum magneticum AMB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TBN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tbm|3tbm]], [[3tbo|3tbo]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amb400, amb4007 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=342108 MAGSA])</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=3tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tbn OCA], [https://pdbe.org/3tbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tbn RCSB], [https://www.ebi.ac.uk/pdbsum/3tbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tbn ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q2W014_MAGSA Q2W014_MAGSA]
-The recently discovered CDGSH iron-sulfur domains (CISDs) are classified into seven major types with a wide distribution throughout the three domains of life. The type 1 protein mitoNEET has been shown to fold into a dimer with the signature CDGSH motif binding to a [2Fe-2S] cluster. However, the structures of all other types of CISDs were unknown. Here we report the crystal structures of type 3, 4, and 6 CISDs determined at 1.5 A, 1.8 A and 1.15 A resolution, respectively. The type 3 and 4 CISD each contain one CDGSH motif and adopt a dimeric structure. Although similar to each other, the two structures have permutated topologies, and both are distinct from the type 1 structure. The type 6 CISD contains tandem CDGSH motifs and adopts a monomeric structure with an internal pseudo dyad symmetry. All currently known CISD structures share dual iron-sulfur binding modules and a beta-sandwich for either intermolecular or intramolecular dimerization. The iron-sulfur binding module, the beta-strand N-terminal to the module and a proline motif are conserved among different type structures, but the dimerization module and the interface and orientation between the two iron-sulfur binding modules are divergent. Sequence analysis further shows resemblance between CISD types 4 and 7 and between 1 and 2. Our findings suggest that all CISDs share common ancestry and diverged into three primary folds with a characteristic phylogenetic distribution: a eukaryote-specific fold adopted by types 1 and 2 proteins, a prokaryote-specific fold adopted by types 3, 4 and 7 proteins, and a tandem-motif fold adopted by types 5 and 6 proteins. Our comprehensive structural, sequential and phylogenetic analysis provides significant insight into the assembly principles and evolutionary relationship of CISDs.
-Structure and Molecular Evolution of CDGSH Iron-Sulfur Domains.,Lin J, Zhang L, Lai S, Ye K PLoS One. 2011;6(9):e24790. Epub 2011 Sep 16. PMID:21949752<ref>PMID:21949752</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3tbn" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Magsa]]
+[[Category: Magnetospirillum magneticum AMB-1]]
-[[Category: Lin, J]]
+[[Category: Lin J]]
-[[Category: Ye, K]]
+[[Category: Ye K]]
-[[Category: Zhang, L]]
+[[Category: Zhang L]]
-[[Category: Cdgsh]]
-[[Category: Iron-sulfur]]
-[[Category: Metal binding protein]]
-[[Category: Miner2]]

3tbn

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Crystal structure of a miner2 homolog: a type 6 CDGSH iron-sulfur protein.

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