5C93
Histidine kinase with ATP
Summary for 5C93
| Entry DOI | 10.2210/pdb5c93/pdb |
| Descriptor | Histidine kinase, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | histidine kinase, atp, transferase |
| Biological source | Lactobacillus plantarum 16 |
| Total number of polymer chains | 2 |
| Total formula weight | 59940.50 |
| Authors | |
| Primary citation | Cai, Y.,Su, M.,Ahmad, A.,Hu, X.,Sang, J.,Kong, L.,Chen, X.,Wang, C.,Shuai, J.,Han, A. Conformational dynamics of the essential sensor histidine kinase WalK. Acta Crystallogr D Struct Biol, 73:793-803, 2017 Cited by PubMed 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. PubMed: 28994408DOI: 10.1107/S2059798317013043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.518 Å) |
Structure validation
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