3EHJ

Crystal structure of DesKC-H188V in complex with AMP-PCP

Summary for 3EHJ

• Entry DOI: 10.2210/pdb3ehj/pdb
• Related: 3EHF 3EHG 3EHH
• Descriptor: Sensor kinase (YocF protein), PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: four-helix bundle, ghl atpase domain, kinase, transferase
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane; Multi-pass membrane protein (Potential): O34757
• Total number of polymer chains: 2
• Total formula weight: 51672.47

Authors

Albanesi, D.,Alzari, P.M.,Buschiazzo, A. (deposition date: 2008-09-12, release date: 2009-09-15, Last modification date: 2024-11-06)

Primary citation

Albanesi, D.,Martin, M.,Trajtenberg, F.,Mansilla, M.C.,Haouz, A.,Alzari, P.M.,de Mendoza, D.,Buschiazzo, A.
Structural plasticity and catalysis regulation of a thermosensor histidine kinase
Proc.Natl.Acad.Sci.USA, 106:16185-16190, 2009

PubMed Abstract: Temperature sensing is essential for the survival of living cells. A major challenge is to understand how a biological thermometer processes thermal information to optimize cellular functions. Using structural and biochemical approaches, we show that the thermosensitive histidine kinase, DesK, from Bacillus subtilis is cold-activated through specific interhelical rearrangements in its central four-helix bundle domain. As revealed by the crystal structures of DesK in different functional states, the plasticity of this helical domain influences the catalytic activities of the protein, either by modifying the mobility of the ATP-binding domains for autokinase activity or by modulating binding of the cognate response regulator to sustain the phosphotransferase and phosphatase activities. The structural and biochemical data suggest a model in which the transmembrane sensor domain of DesK promotes these structural changes through conformational signals transmitted by the membrane-connecting two-helical coiled-coil, ultimately controlling the alternation between output autokinase and phosphatase activities. The structural comparison of the different DesK variants indicates that incoming signals can take the form of helix rotations and asymmetric helical bends similar to those reported for other sensing systems, suggesting that a similar switching mechanism could be operational in a wide range of sensor histidine kinases.

PubMed: 19805278
DOI: 10.1073/pnas.0906699106

Experimental method

X-RAY DIFFRACTION (2.5 Å)