5nfk
From Proteopedia
(Difference between revisions)
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<StructureSection load='5nfk' size='340' side='right'caption='[[5nfk]], [[Resolution|resolution]] 0.98Å' scene=''> | <StructureSection load='5nfk' size='340' side='right'caption='[[5nfk]], [[Resolution|resolution]] 0.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5nfk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NFK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NFK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nfk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinm2 Sinm2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NFK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NFK FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SM2011_c00487 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1286640 SINM2])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nfk OCA], [http://pdbe.org/5nfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nfk RCSB], [http://www.ebi.ac.uk/pdbsum/5nfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nfk ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nfk OCA], [http://pdbe.org/5nfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nfk RCSB], [http://www.ebi.ac.uk/pdbsum/5nfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nfk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sinorhizobium meliloti is a nitrogen-fixing bacterium forming symbiotic nodules with the legume Medicago truncatula. S. meliloti possesses two BolA-like proteins (BolA and YrbA), the function of which is unknown. In organisms where BolA proteins and monothiol glutaredoxins (Grxs) are present, they contribute to the regulation of iron homeostasis by bridging a [2Fe-2S] cluster into heterodimers. A role in the maturation of iron-sulfur (Fe-S) proteins is also attributed to both proteins. In the present study, we have performed a structure-function analysis of SmYrbA showing that it coordinates diverse divalent metal ions (Fe2+, Co2+, Ni2+, Cu2+ and Zn2+) using His32 and His67 residues, that are also used for Fe-S cluster binding in BolA-Grx heterodimers. It also possesses the capacity to form heterodimers with the sole monothiol glutaredoxin (SmGrx2) present in this species. Using cellular approaches analyzing the metal tolerance of S. meliloti mutant strains inactivated in the yrbA and/or bolA genes, we provide evidence for a connection of YrbA with the regulation of iron homeostasis. The mild defects in M. truncatula nodulation reported for the yrbA bolA mutant as compared with the stronger defects in nodule development previously observed for a grx2 mutant suggest functions independent of SmGrx2. These results help in clarifying the physiological role of BolA-type proteins in bacteria. | ||
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| + | Sinorhizobium meliloti YrbA binds divalent metal cations using two conserved histidines.,Roret T, Alloing G, Girardet JM, Perrot T, Dhalleine T, Couturier J, Frendo P, Didierjean C, Rouhier N Biosci Rep. 2020 Oct 30;40(10). pii: 226508. doi: 10.1042/BSR20202956. PMID:32970113<ref>PMID:32970113</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5nfk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Sinm2]] | ||
[[Category: Didierjean, C]] | [[Category: Didierjean, C]] | ||
[[Category: Roret, T]] | [[Category: Roret, T]] | ||
Revision as of 07:59, 2 December 2020
Crystal structure of YrbA from Sinorhizobium meliloti in complex with nickel.
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Categories: Large Structures | Sinm2 | Didierjean, C | Roret, T | Bola | Histidyl ligation | Ligase | Yrba
