ArticleActa crystallographica. Section D, Structural biology2017
Conformational dynamics of the essential sensor histidine kinase WalK.
Article in Acta crystallographica. Section D, Structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Insights Into the Conformational Dynamics of the Cytoplasmic Domain of Metal-Sensing Sensor Histidine Kinase ZraS.Proteins · 2025Article
- Two-Component System Sensor Kinase Inhibitors Target the ATP-Lid of PmrB to Disrupt Colistin Resistance inBiochemistry · 2025Article
- Mechanism of activation and autophosphorylation of a histidine kinase.Communications chemistry · 2024Article
- Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems.Biochemistry · 2023Review
- Insights into the structure and function of the histidine kinase ComP from Bacillus amyloliquefaciens based on molecular modeling.Bioscience reports · 2022Article
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- Recent Advances in Histidine Kinase-Targeted Antimicrobial Agents.Frontiers in chemistry · 2022Review
- The W-Acidic Motif of Histidine Kinase WalK Is Required for Signaling and Transcriptional Regulation inFrontiers in microbiology · 2022Article
- Article
- Article
- Structural asymmetry does not indicate hemiphosphorylation in the bacterial histidine kinase CpxA.The Journal of biological chemistry · 2020Article
- Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Bacteriophytochromes - from informative model systems of phytochrome function to powerful tools in cell biology.Current opinion in structural biology · 2019Review
- Structural insights into the signalling mechanisms of two-component systems.Nature reviews. Microbiology · 2018Review
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Authors and funding
10 authors at 1 institution in 1 country.
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Abstract
Two-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, which regulate RR activity through a phosphorylation and dephosphorylation cycle. However, how SKs perform different enzymatic activities is poorly understood. Here, several crystal structures of the minimal catalytic region of WalK, an essential SK from Lactobacillus plantarum that shares 60% sequence identity with its homologue VicK from Streptococcus mutans, are presented. WalK adopts an asymmetrical closed structure in the presence of ATP or ADP, in which one of the CA domains is positioned close to the DHp domain, thus leading both the β- and γ-phosphates of ATP/ADP to form hydrogen bonds to the ℇ- but not the δ-nitrogen of the phosphorylatable histidine in the DHp domain. In addition, the DHp domain in the ATP/ADP-bound state has a 25.7° asymmetrical helical bending coordinated with the repositioning of the CA domain; these processes are mutually exclusive and alternate in response to helicity changes that are possibly regulated by upstream signals. In the absence of ATP or ADP, however, WalK adopts a completely symmetric open structure with its DHp domain centred between two outward-reaching CA domains. In summary, these structures of WalK reveal the intrinsic dynamic properties of an SK structure as a molecular basis for multifunctionality.
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