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| | <StructureSection load='5nfm' size='340' side='right'caption='[[5nfm]], [[Resolution|resolution]] 0.80Å' scene=''> | | <StructureSection load='5nfm' size='340' side='right'caption='[[5nfm]], [[Resolution|resolution]] 0.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nfm]] 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=5NFM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NFM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti_2011 Sinorhizobium meliloti 2011]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NFM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</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]] 0.8Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene></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=5nfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nfm OCA], [http://pdbe.org/5nfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nfm RCSB], [http://www.ebi.ac.uk/pdbsum/5nfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nfm 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=5nfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nfm OCA], [https://pdbe.org/5nfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nfm RCSB], [https://www.ebi.ac.uk/pdbsum/5nfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nfm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A452CS62_SINM2 A0A452CS62_SINM2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sinm2]] | + | [[Category: Sinorhizobium meliloti 2011]] |
| - | [[Category: Didierjean, C]] | + | [[Category: Didierjean C]] |
| - | [[Category: Roret, T]] | + | [[Category: Roret T]] |
| - | [[Category: Bola]]
| + | |
| - | [[Category: Histidyl ligation]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Yrba]]
| + | |
| Structural highlights
Function
A0A452CS62_SINM2
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roret T, Alloing G, Girardet JM, Perrot T, Dhalleine T, Couturier J, Frendo P, Didierjean C, Rouhier N. Sinorhizobium meliloti YrbA binds divalent metal cations using two conserved histidines. Biosci Rep. 2020 Oct 30;40(10). pii: 226508. doi: 10.1042/BSR20202956. PMID:32970113 doi:http://dx.doi.org/10.1042/BSR20202956
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