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| | <StructureSection load='2vii' size='340' side='right'caption='[[2vii]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='2vii' size='340' side='right'caption='[[2vii]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VII FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VII FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c98|2c98]], [[2bjv|2bjv]], [[2c9c|2c9c]], [[2bjw|2bjw]], [[2c99|2c99]], [[2c96|2c96]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2vii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vii OCA], [https://pdbe.org/2vii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vii RCSB], [https://www.ebi.ac.uk/pdbsum/2vii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vii 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=2vii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vii OCA], [https://pdbe.org/2vii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vii RCSB], [https://www.ebi.ac.uk/pdbsum/2vii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vii 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>
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buck, M]] | + | [[Category: Buck M]] |
| - | [[Category: Joly, N]] | + | [[Category: Joly N]] |
| - | [[Category: Rappas, M]] | + | [[Category: Rappas M]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
| - | [[Category: Aaa]]
| + | |
| - | [[Category: Activator]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Enhancer binding protein]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Pspf]]
| + | |
| - | [[Category: Sigma54 activator]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription activation]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Two-component regulatory system]]
| + | |
| 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
Mechanochemical proteins rely on ATP hydrolysis to establish the different functional states required for their biological output. Studying the transient functional intermediate states these proteins adopt as they progress through the ATP hydrolysis cycle is key to understanding the molecular basis of their mechanism. Many of these intermediates have been successfully 'trapped' and functionally characterised using ATP analogues. Here, we present a new nucleotide analogue, AMP-AlF(x), which traps PspF, a bacterial enhancer binding protein, in a stable complex with the sigma(54)-RNA polymerase holoenzyme. The crystal structure of AMP-AlF(x)*PspF(1-275) provides new information on protein-nucleotide interactions and suggests that the beta and gamma phosphates are more important than the alpha phosphate in terms of sensing nucleotide bound states. In addition, functional data obtained with AMP-AlF(x) establish distinct roles for the conserved catalytic AAA(+) (ATPases associated with various cellular activities) residues, suggesting that AMP-AlF(x) is a powerful new tool to study AAA(+) protein family members and, more generally, Walker motif ATPases.
Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fluoride.,Joly N, Rappas M, Buck M, Zhang X J Mol Biol. 2008 Feb 1;375(5):1206-11. Epub 2007 Nov 22. PMID:18082766[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Joly N, Rappas M, Buck M, Zhang X. Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fluoride. J Mol Biol. 2008 Feb 1;375(5):1206-11. Epub 2007 Nov 22. PMID:18082766 doi:10.1016/j.jmb.2007.11.050
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