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- | {{Seed}} | |
- | [[Image:3c3w.png|left|200px]] | |
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- | <!-- | + | ==Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR== |
- | The line below this paragraph, containing "STRUCTURE_3c3w", creates the "Structure Box" on the page.
| + | <StructureSection load='3c3w' size='340' side='right'caption='[[3c3w]], [[Resolution|resolution]] 2.20Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3c3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C3W FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
- | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | {{STRUCTURE_3c3w| PDB=3c3w | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c3w OCA], [https://pdbe.org/3c3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c3w RCSB], [https://www.ebi.ac.uk/pdbsum/3c3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c3w ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/DEVR_MYCTU DEVR_MYCTU] Member of the two-component regulatory system DevR/DevS (also called DosR/DosS) involved in onset of the dormancy response (PubMed:15033981). Regulates an approximately 48-member regulon (PubMed:12953092, PubMed:11416222, PubMed:15033981, PubMed:18400743). When phosphorylated binds and activates the promoter of DevR regulon genes in response to hypoxia (PubMed:18359816, PubMed:21764934, PubMed:28977726). The presence of target DNA increases stability of phospho-DevR in vitro (PubMed:28977726). Activates its own transcription under hypoxic but not aerobic conditions, probably binds as a dimer to tandem binding sites within the devR and hspX promoters (PubMed:18359816). Accepts a phosphate group from DevS (DosS) and from DosT (PubMed:15033981, PubMed:15073296, PubMed:21764934, PubMed:28977726). Does not regulate transcription of dosT (PubMed:19487478).<ref>PMID:11416222</ref> <ref>PMID:12953092</ref> <ref>PMID:15033981</ref> <ref>PMID:15073296</ref> <ref>PMID:18359816</ref> <ref>PMID:18400743</ref> <ref>PMID:19487478</ref> <ref>PMID:21764934</ref> <ref>PMID:28977726</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/3c3w_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </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=3c3w ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | ===Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR=== | + | ==See Also== |
- | | + | *[[Response regulator 3D structure|Response regulator 3D structure]] |
- | | + | == References == |
- | <!-- | + | <references/> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_18353359}}, adds the Publication Abstract to the page
| + | __TOC__ |
- | (as it appears on PubMed at http://www.pubmed.gov), where 18353359 is the PubMed ID number.
| + | </StructureSection> |
- | -->
| + | [[Category: Large Structures]] |
- | {{ABSTRACT_PUBMED_18353359}}
| + | |
- | | + | |
- | ==About this Structure==
| + | |
- | 3C3W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C3W OCA].
| + | |
- | | + | |
- | ==Reference==
| + | |
- | Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation., Wisedchaisri G, Wu M, Sherman DR, Hol WG, J Mol Biol. 2008 Apr 18;378(1):227-42. Epub 2008 Feb 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18353359 18353359]
| + | |
| [[Category: Mycobacterium tuberculosis]] | | [[Category: Mycobacterium tuberculosis]] |
- | [[Category: Single protein]]
| + | [[Category: Hol WGJ]] |
- | [[Category: Hol, W G.J.]] | + | [[Category: Sherman DR]] |
- | [[Category: Sherman, D R.]] | + | [[Category: Wisedchaisri G]] |
- | [[Category: Wisedchaisri, G.]] | + | [[Category: Wu M]] |
- | [[Category: Wu, M.]] | + | |
- | [[Category: Dna-binding protein]]
| + | |
- | [[Category: Response regulator]]
| + | |
- | [[Category: Transcription]]
| + | |
- | [[Category: Transcription regulation]]
| + | |
- | [[Category: Tuberculosis]]
| + | |
- | [[Category: Two-component regulatory system]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:46:25 2008''
| + | |
| Structural highlights
Function
DEVR_MYCTU Member of the two-component regulatory system DevR/DevS (also called DosR/DosS) involved in onset of the dormancy response (PubMed:15033981). Regulates an approximately 48-member regulon (PubMed:12953092, PubMed:11416222, PubMed:15033981, PubMed:18400743). When phosphorylated binds and activates the promoter of DevR regulon genes in response to hypoxia (PubMed:18359816, PubMed:21764934, PubMed:28977726). The presence of target DNA increases stability of phospho-DevR in vitro (PubMed:28977726). Activates its own transcription under hypoxic but not aerobic conditions, probably binds as a dimer to tandem binding sites within the devR and hspX promoters (PubMed:18359816). Accepts a phosphate group from DevS (DosS) and from DosT (PubMed:15033981, PubMed:15073296, PubMed:21764934, PubMed:28977726). Does not regulate transcription of dosT (PubMed:19487478).[1] [2] [3] [4] [5] [6] [7] [8] [9]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Sherman DR, Voskuil M, Schnappinger D, Liao R, Harrell MI, Schoolnik GK. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7534-9. PMID:11416222 doi:10.1073/pnas.121172498
- ↑ Voskuil MI, Schnappinger D, Visconti KC, Harrell MI, Dolganov GM, Sherman DR, Schoolnik GK. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J Exp Med. 2003 Sep 1;198(5):705-13. PMID:12953092 doi:10.1084/jem.20030205
- ↑ Roberts DM, Liao RP, Wisedchaisri G, Hol WG, Sherman DR. Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J Biol Chem. 2004 May 28;279(22):23082-7. Epub 2004 Mar 19. PMID:15033981 doi:10.1074/jbc.M401230200
- ↑ Saini DK, Malhotra V, Dey D, Pant N, Das TK, Tyagi JS. DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR. Microbiology (Reading). 2004 Apr;150(Pt 4):865-875. PMID:15073296 doi:10.1099/mic.0.26218-0
- ↑ Chauhan S, Tyagi JS. Cooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: implication in the induction of DevR target genes. J Bacteriol. 2008 Jun;190(12):4301-12. PMID:18359816 doi:10.1128/JB.01308-07
- ↑ Kumar A, Deshane JS, Crossman DK, Bolisetty S, Yan BS, Kramnik I, Agarwal A, Steyn AJ. Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon. J Biol Chem. 2008 Jun 27;283(26):18032-9. doi: 10.1074/jbc.M802274200. Epub 2008 , Apr 9. PMID:18400743 doi:10.1074/jbc.M802274200
- ↑ Honaker RW, Leistikow RL, Bartek IL, Voskuil MI. Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy. Infect Immun. 2009 Aug;77(8):3258-63. PMID:19487478 doi:10.1128/IAI.01449-08
- ↑ Gautam US, Sikri K, Tyagi JS. The residue threonine 82 of DevR (DosR) is essential for DevR activation and function in Mycobacterium tuberculosis despite its atypical location. J Bacteriol. 2011 Sep;193(18):4849-58. PMID:21764934 doi:10.1128/JB.05051-11
- ↑ Sousa EHS, Gonzalez G, Gilles-Gonzalez MA. Target DNA stabilizes Mycobacterium tuberculosis DevR/DosR phosphorylation by the full-length oxygen sensors DevS/DosS and DosT. FEBS J. 2017 Nov;284(22):3954-3967. PMID:28977726 doi:10.1111/febs.14284
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