2YKF

Sensor region of a sensor histidine kinase

Summary for 2YKF

• Entry DOI: 10.2210/pdb2ykf/pdb
• Related: 2YKH
• Descriptor: PROBABLE SENSOR HISTIDINE KINASE PDTAS, SULFATE ION, BROMIDE ION, ... (4 entities in total)
• Functional Keywords: transferase, two-component system, gaf domain, pas domain
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 1
• Total formula weight: 33927.36

Authors

Preu, J.,Panjikar, S.,Morth, P.,Jaiswal, R.,Karunakar, P.,Tucker, P.A. (deposition date: 2011-05-26, release date: 2012-06-06, Last modification date: 2024-05-08)

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

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: 22115998
DOI: 10.1016/J.JSB.2011.11.012

Experimental method

X-RAY DIFFRACTION (2 Å)