2wiu

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[[Image:2wiu.png|left|200px]]
 
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==Mercury-modified bacterial persistence regulator hipBA==
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The line below this paragraph, containing "STRUCTURE_2wiu", creates the "Structure Box" on the page.
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<StructureSection load='2wiu' size='340' side='right'caption='[[2wiu]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2wiu]] is a 4 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=2WIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WIU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.35&#8491;</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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{{STRUCTURE_2wiu| PDB=2wiu | SCENE= }}
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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=2wiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wiu OCA], [https://pdbe.org/2wiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wiu RCSB], [https://www.ebi.ac.uk/pdbsum/2wiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wiu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIPA_ECOLI HIPA_ECOLI] Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter.<ref>PMID:17041039</ref> <ref>PMID:6348026</ref> <ref>PMID:8021189</ref> <ref>PMID:14622409</ref> <ref>PMID:19150849</ref>
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wi/2wiu_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=2wiu 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 ==
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Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data.
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===Mercury-modified bacterial persistence regulator hipBA===
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New kinase regulation mechanism found in HipBA: a bacterial persistence switch.,Evdokimov A, Voznesensky I, Fennell K, Anderson M, Smith JF, Fisher DA Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):875-9. Epub 2009, Jul 17. PMID:19622872<ref>PMID:19622872</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 2wiu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19622872}}, adds the Publication Abstract to the page
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19622872 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19622872}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2wiu]] is a 4 chain structure with 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=2WIU OCA].
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==Reference==
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<ref group="xtra">PMID:019622872</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Anderson, M.]]
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[[Category: Anderson M]]
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[[Category: Evdokimov, A.]]
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[[Category: Evdokimov A]]
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[[Category: Fennell, K.]]
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[[Category: Fennell K]]
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[[Category: Fisher, D A.]]
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[[Category: Fisher DA]]
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[[Category: Smith, J F.]]
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[[Category: Smith JF]]
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[[Category: Voznesensky, I.]]
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[[Category: Voznesensky I]]
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[[Category: Dna-binding]]
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[[Category: Mercury derivative]]
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[[Category: Repressor]]
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[[Category: Sad]]
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[[Category: Serine kinase]]
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[[Category: Transcription regulation]]
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[[Category: Transferase transcription complex]]
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[[Category: Transferase-transcription complex]]
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Current revision

Mercury-modified bacterial persistence regulator hipBA

PDB ID 2wiu

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