Crystallographic characterization of a novel protein sixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay

Keisuke Hamada; Masato Kato; Takeshi Mizuno; Toshio Hakoshima

doi:10.1107/S0907444998007756

Crystallographic characterization of a novel protein sixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay

Keisuke Hamada, Masato Kato, Takeshi Mizuno, Toshio Hakoshima

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

1 Scopus citations

Abstract

SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P2₁2₁2₁ with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 Å, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 Å resolution using synchrotron radiation.

Original language	English (US)
Pages (from-to)	269-271
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
Issue number	1
DOIs	https://doi.org/10.1107/S0907444998007756
State	Published - Jan 1 1999

ASJC Scopus subject areas

Structural Biology

Access to Document

10.1107/S0907444998007756

Cite this

Crystallographic characterization of a novel protein sixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay. / Hamada, Keisuke; Kato, Masato; Mizuno, Takeshi et al.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 1, 01.01.1999, p. 269-271.

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

@article{c779f3f46cbf4f3abb93fadcc0cf56e7,

title = "Crystallographic characterization of a novel protein sixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay",

abstract = "SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121 with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 {\AA}, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 {\AA} resolution using synchrotron radiation.",

author = "Keisuke Hamada and Masato Kato and Takeshi Mizuno and Toshio Hakoshima",

year = "1999",

month = jan,

day = "1",

doi = "10.1107/S0907444998007756",

language = "English (US)",

volume = "55",

pages = "269--271",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "John Wiley and Sons Inc.",

number = "1",

}

TY - JOUR

T1 - Crystallographic characterization of a novel protein sixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay

AU - Hamada, Keisuke

AU - Kato, Masato

AU - Mizuno, Takeshi

AU - Hakoshima, Toshio

PY - 1999/1/1

Y1 - 1999/1/1

N2 - SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121 with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 Å, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 Å resolution using synchrotron radiation.

AB - SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121 with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 Å, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 Å resolution using synchrotron radiation.

UR - http://www.scopus.com/inward/record.url?scp=0032922201&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032922201&partnerID=8YFLogxK

U2 - 10.1107/S0907444998007756

DO - 10.1107/S0907444998007756

M3 - Article

C2 - 10089421

AN - SCOPUS:0032922201

SN - 0907-4449

VL - 55

SP - 269

EP - 271

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 1

ER -

Crystallographic characterization of a novel protein sixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this