Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris

Wen Ting Lo; Ko Hsin Chin; Hui Lin Shr; Fei Philip Gao; Ping Chiang Lyu; Andrew H.J. Wang; Shan Ho Chou

doi:10.1107/S1744309106047580

Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris

Wen Ting Lo, Ko Hsin Chin, Hui Lin Shr, Fei Philip Gao, Ping Chiang Lyu, Andrew H.J. Wang, Shan Ho Chou

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

Abstract

Histidine-triad (HIT) proteins are a superfamily of nucleotide hydrolases and transferases that contain a conserved HφHφHφφ motif (where φ is a hydrophobic amino acid) and are found in a variety of organisms. In addition to binding to a variety of nucleotides, other biological functions of the HIT superfamily proteins have been discovered and HIT malfunction has been implicated in several human diseases. Structural studies of HIT superfamily proteins are thus of particular interest. In this manuscript, the cloning, expression, crystallization and preliminary X-ray analysis of XC1015, a HIT protein present in the plant pathogen Xanthomonas campestris pathovar campestris, are reported. The XC1015 crystals diffracted to a resolution of 1.3 Å. They are tetragonal and belong to space group P4₃2 ₁2, with unit-cell parameters a = 40.52, b = 40.52, c = 126.89 Å.

Original language	English
Pages (from-to)	1263-1265
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	12
DOIs	https://doi.org/10.1107/S1744309106047580
Publication status	Published - Dec 2006
Externally published	Yes

Keywords

Histidine triad-like protein
Structural genomics
Xanthomonas campestris

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1107/S1744309106047580

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@article{9f7ec0fb7d264d43a8927ba0ea7e4e25,

title = "Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris",

abstract = "Histidine-triad (HIT) proteins are a superfamily of nucleotide hydrolases and transferases that contain a conserved HφHφHφφ motif (where φ is a hydrophobic amino acid) and are found in a variety of organisms. In addition to binding to a variety of nucleotides, other biological functions of the HIT superfamily proteins have been discovered and HIT malfunction has been implicated in several human diseases. Structural studies of HIT superfamily proteins are thus of particular interest. In this manuscript, the cloning, expression, crystallization and preliminary X-ray analysis of XC1015, a HIT protein present in the plant pathogen Xanthomonas campestris pathovar campestris, are reported. The XC1015 crystals diffracted to a resolution of 1.3 {\AA}. They are tetragonal and belong to space group P432 12, with unit-cell parameters a = 40.52, b = 40.52, c = 126.89 {\AA}.",

keywords = "Histidine triad-like protein, Structural genomics, Xanthomonas campestris",

author = "Lo, {Wen Ting} and Chin, {Ko Hsin} and Shr, {Hui Lin} and Gao, {Fei Philip} and Lyu, {Ping Chiang} and Wang, {Andrew H.J.} and Chou, {Shan Ho}",

year = "2006",

month = dec,

doi = "10.1107/S1744309106047580",

language = "English",

volume = "62",

pages = "1263--1265",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris

AU - Lo, Wen Ting

AU - Chin, Ko Hsin

AU - Shr, Hui Lin

AU - Gao, Fei Philip

AU - Lyu, Ping Chiang

AU - Wang, Andrew H.J.

AU - Chou, Shan Ho

PY - 2006/12

Y1 - 2006/12

N2 - Histidine-triad (HIT) proteins are a superfamily of nucleotide hydrolases and transferases that contain a conserved HφHφHφφ motif (where φ is a hydrophobic amino acid) and are found in a variety of organisms. In addition to binding to a variety of nucleotides, other biological functions of the HIT superfamily proteins have been discovered and HIT malfunction has been implicated in several human diseases. Structural studies of HIT superfamily proteins are thus of particular interest. In this manuscript, the cloning, expression, crystallization and preliminary X-ray analysis of XC1015, a HIT protein present in the plant pathogen Xanthomonas campestris pathovar campestris, are reported. The XC1015 crystals diffracted to a resolution of 1.3 Å. They are tetragonal and belong to space group P432 12, with unit-cell parameters a = 40.52, b = 40.52, c = 126.89 Å.

AB - Histidine-triad (HIT) proteins are a superfamily of nucleotide hydrolases and transferases that contain a conserved HφHφHφφ motif (where φ is a hydrophobic amino acid) and are found in a variety of organisms. In addition to binding to a variety of nucleotides, other biological functions of the HIT superfamily proteins have been discovered and HIT malfunction has been implicated in several human diseases. Structural studies of HIT superfamily proteins are thus of particular interest. In this manuscript, the cloning, expression, crystallization and preliminary X-ray analysis of XC1015, a HIT protein present in the plant pathogen Xanthomonas campestris pathovar campestris, are reported. The XC1015 crystals diffracted to a resolution of 1.3 Å. They are tetragonal and belong to space group P432 12, with unit-cell parameters a = 40.52, b = 40.52, c = 126.89 Å.

KW - Histidine triad-like protein

KW - Structural genomics

KW - Xanthomonas campestris

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JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 12

ER -

Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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