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| | <StructureSection load='4uhs' size='340' side='right'caption='[[4uhs]], [[Resolution|resolution]] 5.00Å' scene=''> | | <StructureSection load='4uhs' size='340' side='right'caption='[[4uhs]], [[Resolution|resolution]] 5.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4uhs]] is a 3 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=4UHS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4UHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uhs]] is a 3 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=4UHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UHS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uhj|4uhj]], [[4uhk|4uhk]], [[4uht|4uht]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://proteopedia.org/fgij/fg.htm?mol=4uhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uhs OCA], [http://pdbe.org/4uhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uhs RCSB], [http://www.ebi.ac.uk/pdbsum/4uhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uhs 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=4uhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uhs OCA], [https://pdbe.org/4uhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uhs RCSB], [https://www.ebi.ac.uk/pdbsum/4uhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uhs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CPXR_ECOLI CPXR_ECOLI]] Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Binds and activates transcription from the degP promoter (PubMed:7883164); binding is enhanced by phosphorylation (PubMed:9401031). This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E (PubMed:7883164), as well as that of CpxP protein. Other downstream effectors may include SrkA (PubMed:23416055).<ref>PMID:23416055</ref> <ref>PMID:7883164</ref> <ref>PMID:9401031</ref> | + | [https://www.uniprot.org/uniprot/CPXR_ECOLI CPXR_ECOLI] Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Binds and activates transcription from the degP promoter (PubMed:7883164); binding is enhanced by phosphorylation (PubMed:9401031). This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E (PubMed:7883164), as well as that of CpxP protein. Other downstream effectors may include SrkA (PubMed:23416055).<ref>PMID:23416055</ref> <ref>PMID:7883164</ref> <ref>PMID:9401031</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alzari, P M.A]] | + | [[Category: Alzari PMA]] |
| - | [[Category: Mechaly, A E]] | + | [[Category: Mechaly AE]] |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
CPXR_ECOLI Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Binds and activates transcription from the degP promoter (PubMed:7883164); binding is enhanced by phosphorylation (PubMed:9401031). This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E (PubMed:7883164), as well as that of CpxP protein. Other downstream effectors may include SrkA (PubMed:23416055).[1] [2] [3]
Publication Abstract from PubMed
The transcriptional regulator CpxR mediates an adaptive response to envelope stress, tightly linked to virulence and antibiotics resistance in several Gammaproteobacteria pathogens. In this work, we integrated crystallographic and small-angle X-ray scattering data to gain insights into the structure and conformational plasticity of CpxR from Escherichia coli. CpxR dimerizes through two alternative interaction surfaces. Moreover, widely different CpxR conformations coexist in solution, from compact to fully extended ones. The possible functional implications of these structural features are discussed.
Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance.,Mechaly AE, Haouz A, Sassoon N, Buschiazzo A, Betton JM, Alzari PM J Struct Biol. 2018 Aug 4. pii: S1047-8477(18)30196-5. doi:, 10.1016/j.jsb.2018.08.001. PMID:30086390[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dorsey-Oresto A, Lu T, Mosel M, Wang X, Salz T, Drlica K, Zhao X. YihE kinase is a central regulator of programmed cell death in bacteria. Cell Rep. 2013 Feb 21;3(2):528-37. doi: 10.1016/j.celrep.2013.01.026. Epub 2013, Feb 14. PMID:23416055 doi:http://dx.doi.org/10.1016/j.celrep.2013.01.026
- ↑ Danese PN, Snyder WB, Cosma CL, Davis LJ, Silhavy TJ. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 1995 Feb 15;9(4):387-98. PMID:7883164
- ↑ Raivio TL, Silhavy TJ. Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J Bacteriol. 1997 Dec;179(24):7724-33. PMID:9401031
- ↑ Mechaly AE, Haouz A, Sassoon N, Buschiazzo A, Betton JM, Alzari PM. Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance. J Struct Biol. 2018 Aug 4. pii: S1047-8477(18)30196-5. doi:, 10.1016/j.jsb.2018.08.001. PMID:30086390 doi:http://dx.doi.org/10.1016/j.jsb.2018.08.001
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