1WN0

Crystal Structure of Histidine-containing Phosphotransfer Protein, ZmHP2, from maize

1WN0 の概要

• エントリーDOI: 10.2210/pdb1wn0/pdb
• 関連するPDBエントリー: 1I5N 1OXB 2A0B
• 分子名称: histidine-containing phosphotransfer protein (2 entities in total)
• 機能のキーワード: four-helix bundle, signaling protein, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64901.93

構造登録者

Sugawara, H.,Kawano, Y.,Hatakeyama, T.,Yamaya, T.,Kamiya, N.,Sakakibara, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-07-24, 公開日: 2005-01-25, 最終更新日: 2024-04-03)

主引用文献

Sugawara, H.,Kawano, Y.,Hatakeyama, T.,Yamaya, T.,Kamiya, N.,Sakakibara, H.
Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize
Protein Sci., 14:202-208, 2005

PubMed Abstract: 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 A 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 Ndelta atoms of the phospho-accepting histidine. It may play a key role in the complex formation of ZmHP2 with receiver domains.

PubMed: 15576555
DOI: 10.1110/ps.041076905

実験手法

X-RAY DIFFRACTION (2.2 Å)