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[[Image:2c98.gif|left|200px]]<br />
<applet load="2c98" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2c98, resolution 1.90&Aring;" />
'''STRUCTURAL BASIS OF THE NUCLEOTIDE DRIVEN CONFORMATIONAL CHANGES IN THE AAA DOMAIN OF TRANSCRIPTION ACTIVATOR PSPF'''<br />


==Overview==
==Structural basis of the nucleotide driven conformational changes in the AAA domain of transcription activator PspF==
Bacterial enhancer-binding proteins (EBP) activate transcription by, hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter, complex. We compare six high resolution structures (&lt;2.1 A) of the AAA(+), domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the, atomic details underpinning the origins of the conformational changes, occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain, respond distinctively to nucleotide binding and hydrolysis, suggesting, functional roles during the hydrolysis cycle, which completely agree with, those derived from activities of PspF mutated at these positions. We, propose a putative atomic switch that is responsible for coupling, structural changes in the nucleotide-binding site to the repositioning of, the sigma(54)-interacting loops. Striking similarities in, nucleotide-specific conformational changes and atomic switch exist between, PspF and the large T antigen helicase, suggesting conservation in the, origin of those events amongst AAA(+) proteins.
<StructureSection load='2c98' size='340' side='right'caption='[[2c98]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2c98]] 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=2C98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C98 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=2c98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c98 OCA], [https://pdbe.org/2c98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c98 RCSB], [https://www.ebi.ac.uk/pdbsum/2c98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c98 ProSAT]</span></td></tr>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c98_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c98 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial enhancer-binding proteins (EBP) activate transcription by hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter complex. We compare six high resolution structures (&lt;2.1 A) of the AAA(+) domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the atomic details underpinning the origins of the conformational changes occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain respond distinctively to nucleotide binding and hydrolysis, suggesting functional roles during the hydrolysis cycle, which completely agree with those derived from activities of PspF mutated at these positions. We propose a putative atomic switch that is responsible for coupling structural changes in the nucleotide-binding site to the repositioning of the sigma(54)-interacting loops. Striking similarities in nucleotide-specific conformational changes and atomic switch exist between PspF and the large T antigen helicase, suggesting conservation in the origin of those events amongst AAA(+) proteins.


==About this Structure==
Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF.,Rappas M, Schumacher J, Niwa H, Buck M, Zhang X J Mol Biol. 2006 Mar 24;357(2):481-92. Epub 2006 Jan 13. PMID:16430918<ref>PMID:16430918</ref>
2C98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C98 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF., Rappas M, Schumacher J, Niwa H, Buck M, Zhang X, J Mol Biol. 2006 Mar 24;357(2):481-92. Epub 2006 Jan 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16430918 16430918]
</div>
[[Category: Escherichia coli]]
<div class="pdbe-citations 2c98" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Buck, M.]]
[[Category: Niwa, H.]]
[[Category: Rappas, M.]]
[[Category: Schumacher, J.]]
[[Category: Zhang, X.]]
[[Category: ADP]]
[[Category: aaa domain]]
[[Category: activator]]
[[Category: atp-binding]]
[[Category: atpase]]
[[Category: bacterial sigma54 activator]]
[[Category: dna-binding]]
[[Category: nucleotide-binding]]
[[Category: sensory transduction]]
[[Category: transcription regulation]]
[[Category: two-component regulatory system]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 14:26:00 2007''
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Buck M]]
[[Category: Niwa H]]
[[Category: Rappas M]]
[[Category: Schumacher J]]
[[Category: Zhang X]]

Latest revision as of 17:10, 13 December 2023

Structural basis of the nucleotide driven conformational changes in the AAA domain of transcription activator PspFStructural basis of the nucleotide driven conformational changes in the AAA domain of transcription activator PspF

Structural highlights

2c98 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Bacterial enhancer-binding proteins (EBP) activate transcription by hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter complex. We compare six high resolution structures (<2.1 A) of the AAA(+) domain of EBP phage shock protein F (PspF) including apo, AMPPNP, Mg(2+)-ATP, and ADP forms. These structures permit a description of the atomic details underpinning the origins of the conformational changes occurring during ATP hydrolysis. Conserved regions of PspF's AAA(+) domain respond distinctively to nucleotide binding and hydrolysis, suggesting functional roles during the hydrolysis cycle, which completely agree with those derived from activities of PspF mutated at these positions. We propose a putative atomic switch that is responsible for coupling structural changes in the nucleotide-binding site to the repositioning of the sigma(54)-interacting loops. Striking similarities in nucleotide-specific conformational changes and atomic switch exist between PspF and the large T antigen helicase, suggesting conservation in the origin of those events amongst AAA(+) proteins.

Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF.,Rappas M, Schumacher J, Niwa H, Buck M, Zhang X J Mol Biol. 2006 Mar 24;357(2):481-92. Epub 2006 Jan 13. PMID:16430918[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ Rappas M, Schumacher J, Niwa H, Buck M, Zhang X. Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF. J Mol Biol. 2006 Mar 24;357(2):481-92. Epub 2006 Jan 13. PMID:16430918 doi:10.1016/j.jmb.2005.12.052

2c98, resolution 1.90Å

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