|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2ykh' size='340' side='right'caption='[[2ykh]], [[Resolution|resolution]] 2.78Å' scene=''> | | <StructureSection load='2ykh' size='340' side='right'caption='[[2ykh]], [[Resolution|resolution]] 2.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ykh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ykh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ykf|2ykf]]</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]] 2.78Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=2ykh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykh OCA], [https://pdbe.org/2ykh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykh RCSB], [https://www.ebi.ac.uk/pdbsum/2ykh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykh ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykh OCA], [http://pdbe.org/2ykh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ykh RCSB], [http://www.ebi.ac.uk/pdbsum/2ykh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PDTAS_MYCTU PDTAS_MYCTU]] Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR. | + | [https://www.uniprot.org/uniprot/PDTAS_MYCTU PDTAS_MYCTU] Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histidine kinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Jaiswal, R]] | + | [[Category: Jaiswal R]] |
| - | [[Category: Karunakar, P]] | + | [[Category: Karunakar P]] |
| - | [[Category: Morth, P]] | + | [[Category: Morth P]] |
| - | [[Category: Panjikar, S]] | + | [[Category: Panjikar S]] |
| - | [[Category: Preu, J]] | + | [[Category: Preu J]] |
| - | [[Category: Tucker, P A]] | + | [[Category: Tucker PA]] |
| - | [[Category: Gaf domain]]
| + | |
| - | [[Category: Pas domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Two-component system]]
| + | |
| Structural highlights
Function
PDTAS_MYCTU Member of the two-component regulatory system pdtaR/pdtaS. Autophosphorylates, probably on a histidine residue, and transfers its phosphate group to pdtaR.
Publication Abstract from PubMed
Two-component systems, a sensor histidine kinase (HK) and a response regulator (RR), are ubiquitous signaling systems that allow prokaryotes to respond to external challenges. HKs normally have sensing modules and highly conserved cytosolic histidine kinase and ATPase domains. The interaction between the activated phosphohistidine and the cognate RR allows an external signal to be passed from the exterior of gram-positive bacteria (GPB) to the cytoplasm. Orthologs of the PdtaS/PdtaR regulatory system, found in most GPB phyla, are unusual in two respects. The HK is not membrane anchored, and the RR acts at the level of transcriptional antitermination. The structure of the complete sensor region of the cytosolic HK, PdtaS, from Mycobacterium tuberculosis consists of closely linked GAF and PAS domains. The structure and sequence analysis suggest that the PdtaS/PdtaR regulatory system is structurally equivalent to the EutW/EutV system regulating ethanolamine catabolism in some phyla but that the effector for the PAS domain is not ethanolamine in the Actinobacteria.
The sensor region of the ubiquitous cytosolic sensor kinase, PdtaS, contains PAS and GAF domain sensing modules.,Preu J, Panjikar S, Morth P, Jaiswal R, Karunakar P, Tucker PA J Struct Biol. 2012 Feb;177(2):498-505. Epub 2011 Nov 17. PMID:22115998[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Preu J, Panjikar S, Morth P, Jaiswal R, Karunakar P, Tucker PA. The sensor region of the ubiquitous cytosolic sensor kinase, PdtaS, contains PAS and GAF domain sensing modules. J Struct Biol. 2012 Feb;177(2):498-505. Epub 2011 Nov 17. PMID:22115998 doi:10.1016/j.jsb.2011.11.012
|