7vqf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7vqf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6l79 6l79]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VQF FirstGlance]. <br> | <table><tr><td colspan='2'>[[7vqf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6l79 6l79]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VQF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7vqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vqf OCA], [https://pdbe.org/7vqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vqf RCSB], [https://www.ebi.ac.uk/pdbsum/7vqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vqf 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=7vqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vqf OCA], [https://pdbe.org/7vqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vqf RCSB], [https://www.ebi.ac.uk/pdbsum/7vqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vqf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 20:30, 29 November 2023
Phenol binding protein, MopRPhenol binding protein, MopR
Structural highlights
Publication Abstract from PubMedThe NtrC family of proteins senses external stimuli and accordingly stimulates stress and virulence pathways via activation of associated sigma54-dependent RNA polymerases. However, the structural determinants that mediate this activation are not well understood. Here, we establish using computational, structural, biochemical and biophysical studies that MopR, an NtrC protein, harbors a dynamic bi-directional electrostatic network that connects the phenol pocket to two distal regions, namely the "G-hinge" and the "allosteric-linker". While the G-hinge influences the entry of phenol into the pocket, the allosteric-linker passes the signal to the downstream ATPase domain. We show that phenol binding induces a rewiring of the electrostatic connections by eliciting dynamic allostery, and demonstrate that perturbation of the core relay residues results in a complete loss of ATPase stimulation. Furthermore, we found a mutation of the G-hinge, approximately 20A from the phenol pocket, promotes altered flexibility by shifting the pattern of conformational states accessed, leading to a protein with 7-fold enhanced phenol binding ability and enhanced transcriptional activation. Finally, we conducted a global analysis which illustrates that dynamic allostery-driven conserved community networks are universal and evolutionarily conserved across species. Taken together, these results provide insights into the mechanisms of dynamic allostery-mediated conformational changes in NtrC sensor proteins. Phenol sensing in nature is modulated via a conformational switch governed by dynamic allostery.,Singh J, Sahil M, Ray S, Dcosta C, Panjikar S, Krishnamoorthy G, Mondal J, Anand R J Biol Chem. 2022 Aug 18:102399. doi: 10.1016/j.jbc.2022.102399. PMID:35988639[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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