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| | ==Crystal structure of CpxAHDC (trigonal form)== | | ==Crystal structure of CpxAHDC (trigonal form)== |
| - | <StructureSection load='4biv' size='340' side='right' caption='[[4biv]], [[Resolution|resolution]] 3.40Å' scene=''> | + | <StructureSection load='4biv' size='340' side='right'caption='[[4biv]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4biv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BIV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BIV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4biv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. The October 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Two-component Systems'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_10 10.2210/rcsb_pdb/mom_2015_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BIV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 3.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4biu|4biu]], [[4biw|4biw]], [[4bix|4bix]], [[4biy|4biy]], [[4biz|4biz]], [[4cb0|4cb0]]</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=4biv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4biv OCA], [https://pdbe.org/4biv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4biv RCSB], [https://www.ebi.ac.uk/pdbsum/4biv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4biv ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
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| - | <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=4biv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4biv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4biv RCSB], [http://www.ebi.ac.uk/pdbsum/4biv PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CPXA_ECOLI CPXA_ECOLI]] This protein is involved in several diverse cellular processes, such as the functioning of acetohydroxyacid synthetase I, in the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid, and the synthesis, translocation, or stability of cell envelope proteins. Activates CpxR by phosphorylation. | + | [https://www.uniprot.org/uniprot/CPXA_ECOLI CPXA_ECOLI] This protein is involved in several diverse cellular processes, such as the functioning of acetohydroxyacid synthetase I, in the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid, and the synthesis, translocation, or stability of cell envelope proteins. Activates CpxR by phosphorylation. |
| | <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 4biv" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Histidine kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Alzari, P M]] | + | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Betton, J M]] | + | [[Category: Two-component Systems]] |
| - | [[Category: Mechaly, A E]] | + | [[Category: Alzari PM]] |
| - | [[Category: Sassoon, N]] | + | [[Category: Betton JM]] |
| - | [[Category: Signal transduction]] | + | [[Category: Mechaly AE]] |
| - | [[Category: Transferase]] | + | [[Category: Sassoon N]] |
| - | [[Category: Two-components system]]
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| Structural highlights
Function
CPXA_ECOLI This protein is involved in several diverse cellular processes, such as the functioning of acetohydroxyacid synthetase I, in the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid, and the synthesis, translocation, or stability of cell envelope proteins. Activates CpxR by phosphorylation.
Publication Abstract from PubMed
Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK alpha-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.
Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.,Mechaly AE, Sassoon N, Betton JM, Alzari PM PLoS Biol. 2014 Jan 28;12(1):e1001776. doi: 10.1371/journal.pbio.1001776., eCollection 2014 Jan. PMID:24492262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mechaly AE, Sassoon N, Betton JM, Alzari PM. Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation. PLoS Biol. 2014 Jan 28;12(1):e1001776. doi: 10.1371/journal.pbio.1001776., eCollection 2014 Jan. PMID:24492262 doi:http://dx.doi.org/10.1371/journal.pbio.1001776
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