Insights into Multistep Phosphorelay from the Crystal Structure of the C-Terminal HPt Domain of ArcB

@article{Kato1997InsightsIM,
  title={Insights into Multistep Phosphorelay from the Crystal Structure of the C-Terminal HPt Domain of ArcB},
  author={Masato Kato and Takeshi Mizuno and Toshiyuki Shimizu and Toshio Hakoshima},
  journal={Cell},
  year={1997},
  volume={88},
  pages={717-723}
}
The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined at 2.06 A resolution. The domain consists of six alpha helices containing a four-helix bundle-folding. The… CONTINUE READING

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Yeast HOG 1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN 1YPD 1SSK 1 “ two - component ” osmosensor

  • F. Posas, S. M. Wurgler-Murphy, T. Maeda, T. C. Thai, H. Saito
  • Cell
  • 1996
Highly Influential
4 Excerpts

A novel 15519

  • K. Ishige, S. Nagasawa, S. Tokishita, T. Mizuno
  • 1994
Highly Influential
13 Excerpts

Practical Protein Crystallography (Tokyo

  • D. E. McRee
  • 1993
Highly Influential
3 Excerpts

Crystallization and preliminary X - ray analysis of a histidine kinase domain of the anaerobic sensor protein ArcB from Escherichia coli

  • K. Ishige, T. Mizuno, T. Shimizu, T. Hakoshima
  • Acta Crystallogr . D
  • 1996

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