2YKH
Sensor region of a sensor histidine kinase
Summary for 2YKH
Entry DOI | 10.2210/pdb2ykh/pdb |
Related | 2YKF |
Descriptor | PROBABLE SENSOR HISTIDINE KINASE PDTAS (2 entities in total) |
Functional Keywords | transferase, two-component system, gaf domain, pas domain |
Biological source | MYCOBACTERIUM TUBERCULOSIS |
Total number of polymer chains | 2 |
Total formula weight | 65105.66 |
Authors | Preu, J.,Panjikar, S.,Morth, P.,Jaiswal, R.,Karunakar, P.,Tucker, P.A. (deposition date: 2011-05-27, release date: 2012-06-06, Last modification date: 2023-12-20) |
Primary citation | Preu, J.,Panjikar, S.,Morth, P.,Jaiswal, R.,Karunakar, P.,Tucker, P.A. The Sensor Region of the Ubiquitous Cytosolic Sensor Kinase, Pdtas, Contains Pas and Gaf Domain Sensing Modules. J.Struct.Biol., 177:498-, 2012 Cited by PubMed Abstract: 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. PubMed: 22115998DOI: 10.1016/J.JSB.2011.11.012 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.78 Å) |
Structure validation
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