Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

C. Tomomori; T. Tanaka; R. Dutta; H. Park; S. K. Saha; Y. Zhu; R. Ishima; D. Liu; K. I. Tong; H. Kurokawa; H. Qian; M. Inouye; M. Ikura

doi:10.1038/11495

Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

C. Tomomori, T. Tanaka, R. Dutta, H. Park, S. K. Saha, Y. Zhu, R. Ishima, D. Liu, K. I. Tong, H. Kurokawa, H. Qian, M. Inouye, M. Ikura

Research output: Contribution to journal › Article › peer-review

197 Citations (Scopus)

Abstract

Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

Original language	English
Pages (from-to)	729-734
Number of pages	6
Journal	Nature Structural Biology
Volume	6
Issue number	8
DOIs	https://doi.org/10.1038/11495
Publication status	Published - 1999 Aug 10
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

Access to Document

10.1038/11495

Fingerprint Dive into the research topics of 'Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ'. Together they form a unique fingerprint.

Cite this

Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. / Tomomori, C.; Tanaka, T.; Dutta, R.; Park, H.; Saha, S. K.; Zhu, Y.; Ishima, R.; Liu, D.; Tong, K. I.; Kurokawa, H.; Qian, H.; Inouye, M.; Ikura, M.

In: Nature Structural Biology, Vol. 6, No. 8, 10.08.1999, p. 729-734.

Research output: Contribution to journal › Article › peer-review

@article{3d9f55d7efc84e4d9627e0f9bf549069,

title = "Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ",

abstract = "Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.",

author = "C. Tomomori and T. Tanaka and R. Dutta and H. Park and Saha, {S. K.} and Y. Zhu and R. Ishima and D. Liu and Tong, {K. I.} and H. Kurokawa and H. Qian and M. Inouye and M. Ikura",

year = "1999",

month = aug,

day = "10",

doi = "10.1038/11495",

language = "English",

volume = "6",

pages = "729--734",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Publishing Group",

number = "8",

}

TY - JOUR

T1 - Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

AU - Tomomori, C.

AU - Tanaka, T.

AU - Dutta, R.

AU - Park, H.

AU - Saha, S. K.

AU - Zhu, Y.

AU - Ishima, R.

AU - Liu, D.

AU - Tong, K. I.

AU - Kurokawa, H.

AU - Qian, H.

AU - Inouye, M.

AU - Ikura, M.

PY - 1999/8/10

Y1 - 1999/8/10

N2 - Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

AB - Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

UR - http://www.scopus.com/inward/record.url?scp=0032804404&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032804404&partnerID=8YFLogxK

U2 - 10.1038/11495

DO - 10.1038/11495

M3 - Article

C2 - 10426948

AN - SCOPUS:0032804404

VL - 6

SP - 729

EP - 734

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 8

ER -