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PMID:19805278

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Citation

Albanesi, D, Martín, M, Trajtenberg, F, Mansilla, MC, Haouz, A, Alzari, PM, de Mendoza, D and Buschiazzo, A (2009) Structural plasticity and catalysis regulation of a thermosensor histidine kinase. Proc. Natl. Acad. Sci. U.S.A. 106:16185-90

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.

Links

PubMed PMC2738621 Online version:10.1073/pnas.0906699106

Keywords

Adenosine Triphosphate/chemistry; Adenosine Triphosphate/metabolism; Amino Acid Substitution; Bacillus subtilis/enzymology; Bacillus subtilis/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites/genetics; Catalysis; Chromatography, Gel; Crystallization; Crystallography, X-Ray; Models, Molecular; Mutation; Protein Binding; Protein Conformation; Protein Kinases/chemistry; Protein Kinases/genetics; Protein Kinases/metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Temperature

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

BACSU:DESR

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O34757

F

Seeded From UniProt

complete

BACSU:DESK

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O34723

F

Seeded From UniProt

complete

BACSU:DESK

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:O34757

F

Seeded From UniProt

complete

BACSU:DESK

GO:0004672: protein kinase activity

ECO:0000314:

F

Fig. 4A The left image shows kinase activity at time intervals at both 25C (top) and 37C (bottom). Kinase activity was up-regulated at lower temperature

complete
CACAO 11195

BACSU:DESK

GO:0004721: phosphoprotein phosphatase activity

ECO:0000314:

F

Fig. 4B Left figure show phosphatase activity of desK at 25C (top) and 37C (bottom).

complete
CACAO 11196

BACSU:DESK

GO:0016740: transferase activity

ECO:0000314:

F

Fig. 4C Figure on the left show phosphotransferase activity of desK at 25C (top) and 37C (bottom).

complete
CACAO 11197

Notes

See also

References

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