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| | ==Crystal structure of E. coli phage shock protein A (PspA 1-144)== | | ==Crystal structure of E. coli phage shock protein A (PspA 1-144)== |
| - | <StructureSection load='4whe' size='340' side='right' caption='[[4whe]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4whe' size='340' side='right'caption='[[4whe]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4whe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WHE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4whe]] 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=4WHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WHE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.8Å</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=4whe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4whe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4whe RCSB], [http://www.ebi.ac.uk/pdbsum/4whe PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4whe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4whe OCA], [https://pdbe.org/4whe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4whe RCSB], [https://www.ebi.ac.uk/pdbsum/4whe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4whe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSPA_ECO57 PSPA_ECO57]] The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp-specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force (By similarity). | + | [https://www.uniprot.org/uniprot/PSPA_ECOLI PSPA_ECOLI] The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp-specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force.<ref>PMID:10629175</ref> <ref>PMID:15485810</ref> <ref>PMID:1712397</ref> <ref>PMID:19804784</ref> <ref>PMID:8598199</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4whe" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brueser, T]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Osadnik, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Parthier, C]] | + | [[Category: Brueser T]] |
| - | [[Category: Schoepfel, M]]
| + | [[Category: Osadnik H]] |
| - | [[Category: Stubbs, M T]]
| + | [[Category: Parthier C]] |
| - | [[Category: Aaa+ protein regulation]] | + | [[Category: Schoepfel M]] |
| - | [[Category: Coiled-coil]] | + | [[Category: Stubbs MT]] |
| - | [[Category: Phage shock response]] | + | |
| - | [[Category: Pspa/im30 family]] | + | |
| - | [[Category: Sigma 54 promoter]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Stress inducible psp system]]
| + | |
| - | [[Category: Transcription initiation]]
| + | |
| - | [[Category: Transcriptional regulation]]
| + | |
| Structural highlights
Function
PSPA_ECOLI The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp-specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Phage shock protein A (PspA) belongs to the highy conserved PspA/IM30 family and is a key component of the stress inducible Psp system in Escherichia coli. One of its central roles is the regulatory interaction with the transcriptional activator of this system, the sigma54 enhancer binding protein PspF, a member of the AAA+ protein family. The PspA/F regulatory system has been intensively studied and serves as a paradigm for AAA+ enzyme regulation by trans-acting factors. However, the molecular mechanism of how exactly PspA controls the activity of PspF and hence sigma54 -dependent expression of the psp genes is still unclear. To approach this question, we identified the minimal PspF-interacting domain of PspA, solved its structure, determined its affinity to PspF and the dissociation kinetics, identified residues that are potentially important for PspF regulation and analyzed effects of their mutation on PspF in vivo and in vitro. Our data indicate that several characteristics of AAA+ regulation in the PspA.F complex resemble those of the AAA+ unfoldase ClpB, with both proteins being regulated by a structurally highly conserved coiled-coil domain. The convergent evolution of both regulatory domains points to a general mechanism to control AAA+ activity for divergent physiological tasks via coiled-coil domains.
The PspF-binding domain PspA and the PspA.F complex - New insights into the coiled-coil dependent regulation of AAA+ proteins.,Osadnik H, Schopfel M, Heidrich E, Mehner D, Lilie H, Parthier C, Risselada HJ, Grubmuller H, Stubbs MT, Bruser T Mol Microbiol. 2015 Aug 3. doi: 10.1111/mmi.13154. PMID:26235546[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dworkin J, Jovanovic G, Model P. The PspA protein of Escherichia coli is a negative regulator of sigma(54)-dependent transcription. J Bacteriol. 2000 Jan;182(2):311-9. PMID:10629175 doi:10.1128/JB.182.2.311-319.2000
- ↑ 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
- ↑ Brissette JL, Weiner L, Ripmaster TL, Model P. Characterization and sequence of the Escherichia coli stress-induced psp operon. J Mol Biol. 1991 Jul 5;220(1):35-48. PMID:1712397 doi:10.1016/0022-2836(91)90379-k
- ↑ 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
- ↑ Kleerebezem M, Crielaard W, Tommassen J. Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions. EMBO J. 1996 Jan 2;15(1):162-71 PMID:8598199
- ↑ Osadnik H, Schopfel M, Heidrich E, Mehner D, Lilie H, Parthier C, Risselada HJ, Grubmuller H, Stubbs MT, Bruser T. The PspF-binding domain PspA and the PspA.F complex - New insights into the coiled-coil dependent regulation of AAA+ proteins. Mol Microbiol. 2015 Aug 3. doi: 10.1111/mmi.13154. PMID:26235546 doi:http://dx.doi.org/10.1111/mmi.13154
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