EC Number   |
|---|
   2.7.13.3 | - |
| 2.7.13.3 | Brucella LOV-HK histidine kinase domain free or in complex with non-hydrolyzable ATP analogue AMP-PCP, mixing of 1 mg/ml protein in 50 mM MES, pH 6.5, and 250 mM sodium chloride, with precipitation solution, X-ray diffraction structure determination and analysis at 2.51 A resolution, molecular modeling |
| 2.7.13.3 | citrate-free or citrate-bound CitA, hanging drop vapor diffusion method, using either 0.1 M HEPES, pH 7.5, 1.6 M (NH4)2SO4, and 5 mM sodium citrate or using 20 mM HEPES, pH 7.5, 0.63 M NaH2PO4 and 0.63 M KH2PO4 |
| 2.7.13.3 | complete cytoplasmic region of enzyme VicK, X-ray diffraction structure determination and analysis |
| 2.7.13.3 | crystal structure at 2.0 A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain P2 of the kinase CheA |
| 2.7.13.3 | crystal structure of the C-terminal HPt domain of ArcB |
| 2.7.13.3 | crystal structure of the CzcS sensor domain in complex with Zn(II) at 1.7 A resolution. The sensor domain is an alpha/beta-fold and senses the Zn(II) stimulus at micromole level in a tetrahedral geometry through its symmetry-related residues His55 and Asp60 on the dimer interface. The sensor domain interacts with the effector with the N-terminal alpha-helices rather than the conserved beta-sheets pocket. The dimerization of the N-terminal H1 and H1' alpha-helices is of primary importance for the activity of histidine kinase activity |
| 2.7.13.3 | crystal structure of the histidine-containing phosphotransfer domain |
| 2.7.13.3 | crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA |
| 2.7.13.3 | crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY |
