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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 [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BJV FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bjw|2bjw]]</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]] 1.7Å</td></tr> |
| - | <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=2bjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjv OCA], [http://pdbe.org/2bjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bjv RCSB], [http://www.ebi.ac.uk/pdbsum/2bjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bjv 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=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 == |
| - | [[http://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> | + | [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]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2bjv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2bjv" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Transcriptional activator|Transcriptional activator]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Beuron, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Bordes, P]] | + | [[Category: Beuron F]] |
| - | [[Category: Buck, M]] | + | [[Category: Bordes P]] |
| - | [[Category: Keetch, C A]] | + | [[Category: Buck M]] |
| - | [[Category: Niwa, H]] | + | [[Category: Keetch CA]] |
| - | [[Category: Rappas, M]] | + | [[Category: Niwa H]] |
| - | [[Category: Robinson, C V]] | + | [[Category: Rappas M]] |
| - | [[Category: Schumacher, J]] | + | [[Category: Robinson CV]] |
| - | [[Category: Wigneshweraraj, S]] | + | [[Category: Schumacher J]] |
| - | [[Category: Zhang, X]] | + | [[Category: Wigneshweraraj S]] |
| - | [[Category: Aaa]]
| + | [[Category: Zhang X]] |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Dna- binding]]
| + | |
| - | [[Category: Enhancer binding protein]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Pspf]]
| + | |
| - | [[Category: Sigma54 activator]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription activation]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
PSPF_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 PubMed
Activators 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
- ↑ Jovanovic G, Weiner L, Model P. Identification, nucleotide sequence, and characterization of PspF, the transcriptional activator of the Escherichia coli stress-induced psp operon. J Bacteriol. 1996 Apr;178(7):1936-45. PMID:8606168
- ↑ Lloyd LJ, Jones SE, Jovanovic G, Gyaneshwar P, Rolfe MD, Thompson A, Hinton JC, Buck M. Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG). J Biol Chem. 2004 Dec 31;279(53):55707-14. Epub 2004 Oct 13. PMID:15485810 doi:10.1074/jbc.M408994200
- ↑ Joly N, Burrows PC, Engl C, Jovanovic G, Buck M. A lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation. J Mol Biol. 2009 Dec 11;394(4):764-75. doi: 10.1016/j.jmb.2009.09.055. Epub 2009 , Oct 3. PMID:19804784 doi:10.1016/j.jmb.2009.09.055
- ↑ Rappas M, Schumacher J, Beuron F, Niwa H, Bordes P, Wigneshweraraj S, Keetch CA, Robinson CV, Buck M, Zhang X. Structural insights into the activity of enhancer-binding proteins. Science. 2005 Mar 25;307(5717):1972-5. PMID:15790859 doi:307/5717/1972
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