1wn0
From Proteopedia
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==Overview== | ==Overview== | ||
| - | In higher plants, histidine-aspartate phosphorelays (two-component system) | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Kamiya, N.]] | [[Category: Kamiya, N.]] | ||
[[Category: Kawano, Y.]] | [[Category: Kawano, Y.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sakakibara, H.]] | [[Category: Sakakibara, H.]] | ||
[[Category: Sugawara, H.]] | [[Category: Sugawara, H.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:07 2008'' |
Revision as of 13:46, 21 February 2008
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Crystal Structure of Histidine-containing Phosphotransfer Protein, ZmHP2, from maize
Overview
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.
About this Structure
1WN0 is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize., Sugawara H, Kawano Y, Hatakeyama T, Yamaya T, Kamiya N, Sakakibara H, Protein Sci. 2005 Jan;14(1):202-8. Epub 2004 Dec 2. PMID:15576555
Page seeded by OCA on Thu Feb 21 15:46:07 2008
Categories: Single protein | Zea mays | Hatakeyama, T. | Kamiya, N. | Kawano, Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakakibara, H. | Sugawara, H. | Yamaya, T. | Four-helix bundle | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Signaling protein | Structural genomics
