2vii

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[[Image:2vii.jpg|left|200px]]
 
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{{Structure
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==PspF1-275-Mg-AMP==
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|PDB= 2vii |SIZE=350|CAPTION= <scene name='initialview01'>2vii</scene>, resolution 2.85&Aring;
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<StructureSection load='2vii' size='340' side='right'caption='[[2vii]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Amp+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Mg+Binding+Site+For+Chain+A'>AC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[2c98|2C98]], [[2bjv|2BJV]], [[2c9c|2C9C]], [[2bjw|2BJW]], [[2c99|2C99]], [[2c96|2C96]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vii OCA], [http://www.ebi.ac.uk/pdbsum/2vii PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vii RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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'''PSPF1-275-MG-AMP'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vii_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2vii ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:18082766</ref>
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2VII is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VII OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18082766 18082766]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2vii" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Buck, M.]]
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[[Category: Joly, N.]]
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[[Category: Rappas, M.]]
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[[Category: Zhang, X.]]
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[[Category: aaa]]
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[[Category: activator]]
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[[Category: atp-binding]]
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[[Category: dna-binding]]
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[[Category: enhancer binding protein]]
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[[Category: gene regulation]]
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[[Category: nucleotide-binding]]
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[[Category: pspf]]
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[[Category: sigma54 activator]]
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[[Category: transcription]]
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[[Category: transcription activation]]
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[[Category: transcription regulation,two-component regulatory system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:42 2008''
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Buck M]]
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[[Category: Joly N]]
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[[Category: Rappas M]]
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[[Category: Zhang X]]

Current revision

PspF1-275-Mg-AMP

PDB ID 2vii

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