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| | <StructureSection load='5e44' size='340' side='right'caption='[[5e44]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='5e44' size='340' side='right'caption='[[5e44]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e44]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_fischeri"_(beijerinck_1889)_bergey_et_al._1930 "achromobacter fischeri" (beijerinck 1889) bergey et al. 1930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E44 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E44 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e44]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_fischeri Aliivibrio fischeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E44 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.65Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fnr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=668 "Achromobacter fischeri" (Beijerinck 1889) Bergey et al. 1930])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=5e44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e44 OCA], [http://pdbe.org/5e44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e44 RCSB], [http://www.ebi.ac.uk/pdbsum/5e44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e44 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=5e44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e44 OCA], [https://pdbe.org/5e44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e44 RCSB], [https://www.ebi.ac.uk/pdbsum/5e44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e44 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q70ET4_ALIFS Q70ET4_ALIFS] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Aliivibrio fischeri]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fontecilla-Camps, J C]] | + | [[Category: Fontecilla-Camps JC]] |
| - | [[Category: Volbeda, A]] | + | [[Category: Volbeda A]] |
| - | [[Category: Labile dimer]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
Q70ET4_ALIFS
Publication Abstract from PubMed
The structure of the dimeric holo-fumarate and nitrate reduction regulator (FNR) from Aliivibrio fischeri has been solved at 2.65 A resolution. FNR globally controls the transition between anaerobic and aerobic respiration in facultative anaerobes through the assembly/degradation of its oxygen-sensitive [4Fe-4S] cluster. In the absence of O2, FNR forms a dimer and specifically binds to DNA, whereas in its presence, the cluster is degraded causing FNR monomerization and DNA dissociation. We have used our crystal structure and the information previously gathered from numerous FNR variants to propose that this process is governed by extremely fine-tuned interactions, mediated by two salt bridges near the amino-terminal cluster-binding domain and an "imperfect" coiled-coil dimer interface. [4Fe-4S] to [2Fe-2S] cluster degradation propagates a conformational signal that indirectly causes monomerization by disrupting the first of these interactions and unleashing the "unzipping" of the FNR dimer in the direction of the carboxyl-terminal DNA binding domain.
The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium.,Volbeda A, Darnault C, Renoux O, Nicolet Y, Fontecilla-Camps JC Sci Adv. 2015 Dec 4;1(11):e1501086. doi: 10.1126/sciadv.1501086. eCollection 2015, Dec. PMID:26665177[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Volbeda A, Darnault C, Renoux O, Nicolet Y, Fontecilla-Camps JC. The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium. Sci Adv. 2015 Dec 4;1(11):e1501086. doi: 10.1126/sciadv.1501086. eCollection 2015, Dec. PMID:26665177 doi:http://dx.doi.org/10.1126/sciadv.1501086
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