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| | <StructureSection load='1ys7' size='340' side='right'caption='[[1ys7]], [[Resolution|resolution]] 1.58Å' scene=''> | | <StructureSection load='1ys7' size='340' side='right'caption='[[1ys7]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ys7]] is a 2 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=1YS7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YS7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ys7]] 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=1YS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YS7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.58Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ys3|1ys3]], [[1ys6|1ys6]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=1ys7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ys7 OCA], [http://pdbe.org/1ys7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ys7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ys7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ys7 ProSAT], [http://www.topsan.org/Proteins/XMTB/1ys7 TOPSAN]</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=1ys7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ys7 OCA], [https://pdbe.org/1ys7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ys7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ys7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ys7 ProSAT], [https://www.topsan.org/Proteins/XMTB/1ys7 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRRA_MYCTU PRRA_MYCTU]] Member of the two-component regulatory system PrrB/PrrA. Involved specifically in early intracellular multiplication of Mycobacterium. | + | [https://www.uniprot.org/uniprot/PRRA_MYCTU PRRA_MYCTU] Member of the two-component regulatory system PrrB/PrrA. Involved specifically in early intracellular multiplication of Mycobacterium. |
| | == 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: Nowak, E]]
| + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Panjikar, S]]
| + | [[Category: Nowak E]] |
| - | [[Category: Tucker, P]]
| + | [[Category: Panjikar S]] |
| - | [[Category: XMTB, Mycobacterium Tuberculosis Structural Proteomics Project]]
| + | [[Category: Tucker P]] |
| - | [[Category: Dna binding domain]]
| + | |
| - | [[Category: Mycobacterium tuberculosis structural proteomics project]] | + | |
| - | [[Category: Phosphorylation]] | + | |
| - | [[Category: Response regulator]] | + | |
| - | [[Category: Structural genomic]] | + | |
| - | [[Category: Transcription regulator]]
| + | |
| - | [[Category: Xmtb]]
| + | |
| Structural highlights
1ys7 is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.58Å |
| Ligands: | , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
PRRA_MYCTU Member of the two-component regulatory system PrrB/PrrA. Involved specifically in early intracellular multiplication of Mycobacterium.
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
The structure of the two-domain response regulator PrrA from Mycobacterium tuberculosis shows a compact structure in the crystal with a well defined interdomain interface. The interface, which does not include the interdomain linker, makes the recognition helix and the trans-activation loop of the effector domain inaccessible for interaction with DNA. Part of the interface involves hydrogen-bonding interactions of a tyrosine residue in the receiver domain that is believed to be involved in signal transduction, which, if disrupted, would destabilize the interdomain interface, allowing a more extended conformation of the molecule, which would in turn allow access to the recognition helix. In solution, there is evidence for an equilibrium between compact and extended forms of the protein that is far toward the compact form when the protein is inactivated but moves toward a more extended form when activated by the cognate sensor kinase PrrB.
The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis.,Nowak E, Panjikar S, Konarev P, Svergun DI, Tucker PA J Biol Chem. 2006 Apr 7;281(14):9659-66. Epub 2006 Jan 23. PMID:16434396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nowak E, Panjikar S, Konarev P, Svergun DI, Tucker PA. The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis. J Biol Chem. 2006 Apr 7;281(14):9659-66. Epub 2006 Jan 23. PMID:16434396 doi:10.1074/jbc.M512004200
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