1zyl
From Proteopedia
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<StructureSection load='1zyl' size='340' side='right'caption='[[1zyl]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1zyl' size='340' side='right'caption='[[1zyl]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1zyl]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1zyl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZYL FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=1zyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zyl OCA], [https://pdbe.org/1zyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zyl RCSB], [https://www.ebi.ac.uk/pdbsum/1zyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zyl ProSAT], [https://www.topsan.org/Proteins/BSGI/1zyl TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/SRKA_ECOLI SRKA_ECOLI] A protein kinase that (auto)phosphorylates on Ser and Thr residues (PubMed:17302814). Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Protects cells from stress by antagonizing the MazE-MazF TA module, probably indirectly as it has not been seen to phosphorylate MazE, MazF or MazG (PubMed:23416055). Probably involved in the extracytoplasmic stress response (PubMed:9159398).[HAMAP-Rule:MF_01497]<ref>PMID:17302814</ref> <ref>PMID:23416055</ref> <ref>PMID:9159398</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1zyl ConSurf]. | </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=1zyl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The Cpx signalling system of Escherichia coli and Salmonella enterica senses extracytoplasmic stress and controls expression of factors that allow the bacterium to adapt to these stressors and thereby enhance survival. Many of the Cpx-responsive genes products are of unknown function. We determined the crystal structure of one of these gene products, called YihE in E. coli, which exhibits a eukaryotic kinase fold. Functional assays established that both YihE and the S. enterica YihE homologue, RdoA, undergo autophosphorylation and phosphorylate protein substrates at Ser/Thr residues in vitro, demonstrating that YihE/RdoA is a novel Ser/Thr protein kinase in prokaryotic cells. Phenotypic analysis of yihE/rdoA null strains indicates that this kinase is most abundant in stationary phase, and is important for long-term cell survival and for expression of surface appendages in both a Cpx-independent and -dependent manner. YihE/RdoA is therefore a previously unknown kinase component of a new type of bacterial phosphorelay mechanism, adding kinase activity as another response to the Cpx sensing system that functions to maintain cellular homeostasis. | ||
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| - | Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway.,Zheng J, He C, Singh VK, Martin NL, Jia Z Mol Microbiol. 2007 Mar;63(5):1360-71. PMID:17302814<ref>PMID:17302814</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1zyl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Jia Z]] | |
| - | [[Category: Jia | + | [[Category: Zheng J]] |
| - | [[Category: Zheng | + | |
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Current revision
Crystal Structure of Hypothetical Protein YihE from Escherichia coli
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