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3qzc

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Current revision (10:51, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qzc' size='340' side='right'caption='[[3qzc]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='3qzc' size='340' side='right'caption='[[3qzc]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qzc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QZC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qzc]] is a 2 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=3QZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QZC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4484, cpxP, JW5558, yiiO ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3qzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qzc OCA], [https://pdbe.org/3qzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qzc RCSB], [https://www.ebi.ac.uk/pdbsum/3qzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qzc 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=3qzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qzc OCA], [https://pdbe.org/3qzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qzc RCSB], [https://www.ebi.ac.uk/pdbsum/3qzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qzc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CPXP_ECOLI CPXP_ECOLI]] Aids in combating extracytoplasmic protein-mediated toxicity.
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[https://www.uniprot.org/uniprot/CPXP_ECOLI CPXP_ECOLI] Aids in combating extracytoplasmic protein-mediated toxicity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CpxP is a novel bacterial periplasmic protein with no homologues of known function. In Gram-negative enteric bacteria, CpxP is thought to interact with the two-component sensor kinase, CpxA, to inhibit induction of the Cpx envelope stress response in the absence of protein misfolding. CpxP has also been shown to facilitate DegP-mediated proteolysis of misfolded proteins. Six mutations that negate the ability of CpxP to function as a signaling protein are localized in or near two conserved LTXXQ motifs that define a class of proteins with similarity to CpxP, Pfam PF07813. To gain insight into how these mutations might affect CpxP signaling and/or proteolytic adaptor functions, the crystal structure of CpxP from Escherichia coli was determined to 2.85 A resolution. The structure revealed an antiparallel dimer of intertwined alpha-helices with a highly basic concave surface. Each protomer consists of a long, hooked and bent hairpin fold with the conserved LTXXQ motifs forming two diverging turns at one end. Biochemical studies demonstrated that CpxP maintains a dimeric state, but may undergo a slight structural adjustment in response to the inducing cue, alkaline pH. Three of the six previously characterized cpxP loss-of-function mutations, M59T, Q55P, and Q128H, likely result from a destabilization of the protein fold, whereas the R60Q, D61E, and D61V mutations may alter intermolecular interactions.
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Structure of the periplasmic stress response protein CpxP.,Thede GL, Arthur DC, Edwards RA, Buelow DR, Wong JL, Raivio TL, Glover JN J Bacteriol. 2011 Feb 11. PMID:21317318<ref>PMID:21317318</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qzc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Edwards, R A]]
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[[Category: Edwards RA]]
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[[Category: Glover, J N.M]]
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[[Category: Glover JNM]]
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[[Category: Thede, G L]]
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[[Category: Thede GL]]
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[[Category: Alpha-helical hairpin]]
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[[Category: Ltxxq motif]]
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[[Category: Signaling protein]]
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[[Category: Stress response regulator]]
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Current revision

Structure of the periplasmic stress response protein CpxP

PDB ID 3qzc

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