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| | <StructureSection load='1zlj' size='340' side='right'caption='[[1zlj]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1zlj' size='340' side='right'caption='[[1zlj]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zlj]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZLJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zlj]] is a 8 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=1ZLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZLJ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zlk|1zlk]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dosR, devR, Rv3133c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=1zlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zlj OCA], [https://pdbe.org/1zlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zlj RCSB], [https://www.ebi.ac.uk/pdbsum/1zlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zlj ProSAT]</span></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=1zlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zlj OCA], [http://pdbe.org/1zlj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zlj RCSB], [http://www.ebi.ac.uk/pdbsum/1zlj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zlj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/R4MI41_MYCTX R4MI41_MYCTX] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hol, W G.J]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Rice, A E]] | + | [[Category: Hol WGJ]] |
| - | [[Category: Roberts, D M]] | + | [[Category: Rice AE]] |
| - | [[Category: Sherman, D R]] | + | [[Category: Roberts DM]] |
| - | [[Category: Wisedchaisri, G]] | + | [[Category: Sherman DR]] |
| - | [[Category: Wu, M]] | + | [[Category: Wisedchaisri G]] |
| - | [[Category: Helix-turn-helix]]
| + | [[Category: Wu M]] |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
R4MI41_MYCTX
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
On encountering low oxygen conditions, DosR activates the transcription of 47 genes, promoting long-term survival of Mycobacterium tuberculosis in a non-replicating state. Here, we report the crystal structures of the DosR C-terminal domain and its complex with a consensus DNA sequence of the hypoxia-induced gene promoter. The DosR C-terminal domain contains four alpha-helices and forms tetramers consisting of two dimers with non-intersecting dyads. In the DNA-bound structure, each DosR C-terminal domain in a dimer places its DNA-binding helix deep into the major groove, causing two bends in the DNA. DosR makes numerous protein-DNA base contacts using only three amino acid residues per subunit: Lys179, Lys182, and Asn183. The DosR tetramer is unique among response regulators with known structures.
Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency.,Wisedchaisri G, Wu M, Rice AE, Roberts DM, Sherman DR, Hol WG J Mol Biol. 2005 Dec 2;354(3):630-41. Epub 2005 Oct 3. PMID:16246368[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wisedchaisri G, Wu M, Rice AE, Roberts DM, Sherman DR, Hol WG. Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency. J Mol Biol. 2005 Dec 2;354(3):630-41. Epub 2005 Oct 3. PMID:16246368 doi:10.1016/j.jmb.2005.09.048
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