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Published online before print December 2, 2004, 10.1110/ps.041076905
Protein Science (2005), 14:202-208. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize

Hajime Sugawara1, Yoshiaki Kawano2, Tomomitsu Hatakeyama3, Tomoyuki Yamaya1, Nobuo Kamiya2 and Hitoshi Sakakibara1

1 Laboratory for Communication Mechanisms, RIKEN Plant Science Center, Yokohama 230-0045, Japan
2 Division of Bio-crystallography Technology, RIKEN Harima Institute, Hyogo 679-5148, Japan
3 Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Nagasaki 852-8521, Japan

(RECEIVED August 30, 2004; FINAL REVISION September 14, 2004; ACCEPTED September 14, 2004)

In higher plants, histidine-aspartate phosphorelays (two-component system) are involved in hormone signaling and stress responses. In these systems, histidine-containing phosphotransfer (HPt) proteins mediate the signal transmission from sensory histidine kinases to response regulators, including integration of several signaling pathways or branching into different pathways. We have determined the crystal structure of a maize HPt protein, ZmHP2, at 2.2 Å resolution. ZmHP2 has six {alpha}-helices with a four-helix bundle at the C-terminus, a feature commonly found in HPt domains. In ZmHP2, almost all of the conserved residues among plant HPt proteins surround this histidine, probably forming the docking interface for the receiver domain of histidine kinase or the response regulator. Arg102 of ZmHP2 is conserved as a basic residue in plant HPt proteins. In bacteria, it is replaced by glutamine or glutamate that form a hydrogen bond to N{delta} atoms of the phospho-accepting histidine. It may play a key role in the complex formation of ZmHP2 with receiver domains.

Keywords: histidine-containing phosphotransfer protein; crystal structure; four-helix bundle; two-component system; Zea mays

Abbreviations: HPt, histidine-containing phosphotransfer protein • HK, histidine kinase • RR, response regulator • RMSD, root mean square deviation • SeMet, selenomethionine-labeled • NCS, noncrystallographic symmetry

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041076905.

Reprint requests to: Hajime Sugawara, Laboratory for Communication Mechanisms, RIKEN Plant Science Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan; e-mail: sugawara{at}psc.riken.go.jp; fax: +81-45-503-9609.


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