3T8Y
Crystal structure of the response regulator domain of Thermotoga maritima CheB
Summary for 3T8Y
| Entry DOI | 10.2210/pdb3t8y/pdb |
| Descriptor | Chemotaxis response regulator protein-glutamate methylesterase, LEAD (II) ION (3 entities in total) |
| Functional Keywords | response regulator, chea, hydrolase |
| Biological source | Thermotoga maritima |
| Cellular location | Cytoplasm (By similarity): Q9WYN9 |
| Total number of polymer chains | 2 |
| Total formula weight | 36775.02 |
| Authors | Park, S.Y.,Crane, B.R. (deposition date: 2011-08-02, release date: 2011-09-14, Last modification date: 2024-03-20) |
| Primary citation | Park, S.Y.,Crane, B.R. Structural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterparts Int.J.Biol.Macromol., 49:794-800, 2011 Cited by PubMed Abstract: CheA-mediated CheB phosphorylation and the subsequent CheB-mediated demethylation of the chemoreceptors are important steps required for the bacterial chemotactic adaptation response. Although Escherichia coli CheB has been reported to interact with CheA competitively against CheY, we have observed that Thermotoga maritima CheB has no detectable CheA-binding. By determining the CheY-like domain crystal structure of T. maritima CheB, and comparing against the T. maritima CheY and Salmonella typhimurium CheB structures, we propose that the two consecutive glutamates in the β4/α4 loop of T. maritima CheB that is absent in T. maritima CheY and in E. coli/S. typhimurium CheB may be one factor contributing to the low CheA affinity. PubMed: 21816169DOI: 10.1016/j.ijbiomac.2011.07.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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