The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Mechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor Domains
Open accessAbstract
Two-component systems (TCSs) are important for the adaptation and survival of bacteria and fungi under stress conditions. A TCS is often composed of a membrane-bound sensor histidine kinase (SK) and a response regulator (RR), which are relayed through sequential phosphorylation steps. However, the mechanism for how an SK is switched on in response to environmental stimuli remains obscure. Here, we report the crystal structure of a complete cytoplasmic portion of an SK, VicK from Streptococcus mutans. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. Moreover, a conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Together, the elegant architecture of VicK with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation.
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PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., Martin, J., Schultz, J. E., Lupas, A. N., & Coles, M. (2006) · Cell · doi:10.1016/j.cell.2006.06.058 · Cited by 416
Cited by
Molecular Mechanisms of Two-Component Signal Transduction
Zschiedrich, C. P., Keidel, V., & Szurmant, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.003 · Cited by 540
Structural insights into the signalling mechanisms of two-component systems
Jacob-Dubuisson, F., Mechaly, A., Betton, J.-M., & Antoine, R. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0055-7 · Cited by 308
Mahapatra, N., Mahanta, P., Pandey, S., & Acharya, R. (2025) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26819 · Cited by 2
A Designed Zn 2+ Sensor Domain Transmits Binding Information to Transmembrane Histidine Kinases
Hatstat, A. K., Kormos, R., Xu, V., Du, G., Liu, L., Zhang, S.-Q., & DeGrado, W. F. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c02273 · Cited by 1
Metadata
- Authors
- Wang, C., Sang, J., Wang, J., Su, M., Downey, J. S., Wu, Q., Wang, S., Cai, Y., Xu, X., Wu, J., Senadheera, D. B., Cvitkovitch, D. G., Chen, L., Goodman, S. D., & Han, A.
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-02-26
- Volume
- 11
- Issue
- 2
- Pages
- e1001493
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- OpenAlex
- W2137799017
- Cited by
- 167
- References
- 3
- FWCI
- 11.53
- Type
- journal article
- Language
- en
- Open access
- gold
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- Wang, C., Sang, J., Wang, J., Su, M., Downey, J. S., Wu, Q., Wang, S., Cai, Y., Xu, X., Wu, J., Senadheera, D. B., Cvitkovitch, D. G., Chen, L., Goodman, S. D., & Han, A. (2013). Mechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor Domains. PLoS Biology. https://doi.org/10.1371/journal.pbio.1001493
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