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==Crystal Structure of PspF(1-275) R168A mutant== | ==Crystal Structure of PspF(1-275) R168A mutant== | ||
<StructureSection load='2bjv' size='340' side='right' caption='[[2bjv]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2bjv' size='340' side='right'caption='[[2bjv]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bjv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2bjv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjv OCA], [https://pdbe.org/2bjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bjv RCSB], [https://www.ebi.ac.uk/pdbsum/2bjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PSPF_ECOLI PSPF_ECOLI] Transcriptional activator for the phage shock protein (psp) operon (pspABCDE) and pspG gene.<ref>PMID:8606168</ref> <ref>PMID:15485810</ref> <ref>PMID:19804784</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 28: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 2bjv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2bjv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Beuron | [[Category: Large Structures]] | ||
[[Category: Bordes | [[Category: Beuron F]] | ||
[[Category: Buck | [[Category: Bordes P]] | ||
[[Category: Keetch | [[Category: Buck M]] | ||
[[Category: Niwa | [[Category: Keetch CA]] | ||
[[Category: Rappas | [[Category: Niwa H]] | ||
[[Category: Robinson | [[Category: Rappas M]] | ||
[[Category: Schumacher | [[Category: Robinson CV]] | ||
[[Category: Wigneshweraraj | [[Category: Schumacher J]] | ||
[[Category: Zhang | [[Category: Wigneshweraraj S]] | ||
[[Category: Zhang X]] | |||
Latest revision as of 12:16, 9 May 2024
Crystal Structure of PspF(1-275) R168A mutantCrystal Structure of PspF(1-275) R168A mutant
Structural highlights
FunctionPSPF_ECOLI Transcriptional activator for the phage shock protein (psp) operon (pspABCDE) and pspG gene.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedActivators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54. Structural insights into the activity of enhancer-binding proteins.,Rappas M, Schumacher J, Beuron F, Niwa H, Bordes P, Wigneshweraraj S, Keetch CA, Robinson CV, Buck M, Zhang X Science. 2005 Mar 25;307(5717):1972-5. PMID:15790859[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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