caa a22 4500 445325437 CHVBK 20180317142718.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s10858-011-9540-2 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9540-2 The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima [Elektronische Daten] [Anh Vu, Damon Hamel, Hongjun Zhou, Frederick Dahlquist] The bacterial histidine autokinase CheA contains a histidine phosphotransfer (Hpt) domain that accepts a phosphate from the catalytic domain and donates the phosphate to either target response regulator protein, CheY or CheB. The Hpt domain forms a helix-bundle structure with a conserved four-helix bundle motif and a variable fifth helix. Observation of two nearly equally populated conformations in the crystal structure of a Hpt domain fragment of CheA from Thermotoga maritima containing only the first four helices suggests more mobility in a tightly packed helix bundle structure than previously thought. In order to examine how the structures of Hpt domain homologs may differ from each other particularly in the conformation of the last helix, and whether an alternative conformation exists in the intact Hpt domain in solution, we have solved a high-resolution, solution structure of the CheA Hpt from T. maritima and characterized the backbone dynamics of this protein. The structure contains a four-helix bundle characteristic of histidine phosphotransfer domains. The position and orientation of the fifth helix resembles those in known Hpt domain crystal and solution structures in other histidine kinases. The alternative conformation that was reported in the crystal structure of the CheA Hpt from T. maritima missing the fifth helix is not detected in the solution structure, suggesting a role for the fifth helix in providing stabilizing forces to the overall structure. The Author(s), 2011 Two component nationallicence CheA nationallicence Histidine phosphotransfer nationallicence Chemotaxis nationallicence Four helix bundle nationallicence Histidine kinase nationallicence Vu Anh Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut Hamel Damon Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut Zhou Hongjun Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut Dahlquist Frederick Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 49-55 0925-2738 51:1-2<49 2011 51 10858 https://doi.org/10.1007/s10858-011-9540-2 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9540-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Vu Anh Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut NATIONALLICENCE 700 1- Hamel Damon Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut NATIONALLICENCE 700 1- Zhou Hongjun Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut NATIONALLICENCE 700 1- Dahlquist Frederick Department of Chemistry and Biochemistry, University of California Santa Barbara, 93103, Santa Barbara, CA, USA aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 49-55 0925-2738 51:1-2<49 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer