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4omz

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==Crystal Structure of NolR from Sinorhizobium fredii==
==Crystal Structure of NolR from Sinorhizobium fredii==
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<StructureSection load='4omz' size='340' side='right' caption='[[4omz]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
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<StructureSection load='4omz' size='340' side='right'caption='[[4omz]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4omz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35423 Atcc 35423]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OMZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4omz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_fredii Sinorhizobium fredii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.64&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nolR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=380 ATCC 35423])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<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=4omz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omz OCA], [http://pdbe.org/4omz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4omz RCSB], [http://www.ebi.ac.uk/pdbsum/4omz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4omz ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4omz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omz OCA], [https://pdbe.org/4omz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omz RCSB], [https://www.ebi.ac.uk/pdbsum/4omz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q83TD2_RHIFR Q83TD2_RHIFR]
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The symbiosis between rhizobial microbes and host plants involves the coordinated expression of multiple genes, which leads to nodule formation and nitrogen fixation. As part of the transcriptional machinery for nodulation and symbiosis across a range of Rhizobium, NolR serves as a global regulatory protein. Here, we present the X-ray crystal structures of NolR in the unliganded form and complexed with two different 22-base pair (bp) double-stranded operator sequences (oligos AT and AA). Structural and biochemical analysis of NolR reveals protein-DNA interactions with an asymmetric operator site and defines a mechanism for conformational switching of a key residue (Gln56) to accommodate variation in target DNA sequences from diverse rhizobial genes for nodulation and symbiosis. This conformational switching alters the energetic contributions to DNA binding without changes in affinity for the target sequence. Two possible models for the role of NolR in the regulation of different nodulation and symbiosis genes are proposed. To our knowledge, these studies provide the first structural insight on the regulation of genes involved in the agriculturally and ecologically important symbiosis of microbes and plants that leads to nodule formation and nitrogen fixation.
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Structural basis for regulation of rhizobial nodulation and symbiosis gene expression by the regulatory protein NolR.,Lee SG, Krishnan HB, Jez JM Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6509-14. doi:, 10.1073/pnas.1402243111. Epub 2014 Apr 14. PMID:24733893<ref>PMID:24733893</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4omz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 35423]]
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[[Category: Large Structures]]
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[[Category: Jez, J M]]
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[[Category: Sinorhizobium fredii]]
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[[Category: Krishnan, H B]]
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[[Category: Jez JM]]
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[[Category: Lee, S G]]
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[[Category: Krishnan HB]]
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[[Category: Helix-turn-helix]]
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[[Category: Lee SG]]
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[[Category: Transcription]]
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[[Category: Transcription regulator]]
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Current revision

Crystal Structure of NolR from Sinorhizobium fredii

PDB ID 4omz

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