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Title: Crystallization of a newly discovered histidine acid phosphatase from Francisella tularensis

Abstract

A histidine acid phosphatase from the CDC Category A pathogen F. tularensis has been crystallized in space group P4{sub 1}2{sub 1}2, with unit-cell parameters a = 61.96, c = 210.78 Å. A 1.75 Å resolution data set was collected at Advanced Light Source beamline 4.2.2. Francisella tularensis is a highly infectious bacterial pathogen that is considered by the Centers for Disease Control and Prevention to be a potential bioterrorism weapon. Here, the crystallization of a 37.2 kDa phosphatase encoded by the genome of F. tularensis subsp. holarctica live vaccine strain is reported. This enzyme shares 41% amino-acid sequence identity with Legionella pneumophila major acid phosphatase and contains the RHGXRXP motif that is characteristic of the histidine acid phosphatase family. Large diffraction-quality crystals were grown in the presence of Tacsimate, HEPES and PEG 3350. The crystals belong to space group P4{sub 1}2{sub 1}2, with unit-cell parameters a = 61.96, c = 210.78 Å. The asymmetric unit is predicted to contain one protein molecule, with a solvent content of 53%. A 1.75 Å resolution native data set was recorded at beamline 4.2.2 of the Lawrence Berkeley National Laboratory Advanced Light Source. Molecular-replacement trials using the human prostatic acid phosphatase structure as themore » search model (28% amino-acid sequence identity) did not produce a satisfactory solution. Therefore, the structure of F. tularensis histidine acid phosphatase will be determined by multiwavelength anomalous dispersion phasing using a selenomethionyl derivative.« less

Authors:
 [1];  [2];  [3];  [2];  [1];  [3]
  1. Department of Chemistry, University of Missouri-Columbia, Columbia, Missouri 65211 (United States)
  2. Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Missouri-Columbia, Columbia, Missouri 65212 (United States)
  3. (United States)
Publication Date:
OSTI Identifier:
22356247
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 1; Other Information: PMCID: PMC2150932; PMID: 16511256; PUBLISHER-ID: ll5042; OAI: oai:pubmedcentral.nih.gov:2150932; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; HISTIDINE; MATHEMATICAL SOLUTIONS; MOLECULES; POTENTIALS; RESOLUTION; SOLUTIONS; SOLVENTS; SPACE GROUPS; STRAINS

Citation Formats

Felts, Richard L., Reilly, Thomas J., Veterinary Medical Diagnostic Laboratory, College of Veterinary Medicine, University of Missouri-Columbia, Columbia, Missouri 65212, Calcutt, Michael J., Tanner, John J., E-mail: tannerjj@missouri.edu, and Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211. Crystallization of a newly discovered histidine acid phosphatase from Francisella tularensis. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309105039813.
Felts, Richard L., Reilly, Thomas J., Veterinary Medical Diagnostic Laboratory, College of Veterinary Medicine, University of Missouri-Columbia, Columbia, Missouri 65212, Calcutt, Michael J., Tanner, John J., E-mail: tannerjj@missouri.edu, & Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211. Crystallization of a newly discovered histidine acid phosphatase from Francisella tularensis. United Kingdom. doi:10.1107/S1744309105039813.
Felts, Richard L., Reilly, Thomas J., Veterinary Medical Diagnostic Laboratory, College of Veterinary Medicine, University of Missouri-Columbia, Columbia, Missouri 65212, Calcutt, Michael J., Tanner, John J., E-mail: tannerjj@missouri.edu, and Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211. Sun . "Crystallization of a newly discovered histidine acid phosphatase from Francisella tularensis". United Kingdom. doi:10.1107/S1744309105039813.
@article{osti_22356247,
title = {Crystallization of a newly discovered histidine acid phosphatase from Francisella tularensis},
author = {Felts, Richard L. and Reilly, Thomas J. and Veterinary Medical Diagnostic Laboratory, College of Veterinary Medicine, University of Missouri-Columbia, Columbia, Missouri 65212 and Calcutt, Michael J. and Tanner, John J., E-mail: tannerjj@missouri.edu and Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211},
abstractNote = {A histidine acid phosphatase from the CDC Category A pathogen F. tularensis has been crystallized in space group P4{sub 1}2{sub 1}2, with unit-cell parameters a = 61.96, c = 210.78 Å. A 1.75 Å resolution data set was collected at Advanced Light Source beamline 4.2.2. Francisella tularensis is a highly infectious bacterial pathogen that is considered by the Centers for Disease Control and Prevention to be a potential bioterrorism weapon. Here, the crystallization of a 37.2 kDa phosphatase encoded by the genome of F. tularensis subsp. holarctica live vaccine strain is reported. This enzyme shares 41% amino-acid sequence identity with Legionella pneumophila major acid phosphatase and contains the RHGXRXP motif that is characteristic of the histidine acid phosphatase family. Large diffraction-quality crystals were grown in the presence of Tacsimate, HEPES and PEG 3350. The crystals belong to space group P4{sub 1}2{sub 1}2, with unit-cell parameters a = 61.96, c = 210.78 Å. The asymmetric unit is predicted to contain one protein molecule, with a solvent content of 53%. A 1.75 Å resolution native data set was recorded at beamline 4.2.2 of the Lawrence Berkeley National Laboratory Advanced Light Source. Molecular-replacement trials using the human prostatic acid phosphatase structure as the search model (28% amino-acid sequence identity) did not produce a satisfactory solution. Therefore, the structure of F. tularensis histidine acid phosphatase will be determined by multiwavelength anomalous dispersion phasing using a selenomethionyl derivative.},
doi = {10.1107/S1744309105039813},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 62,
place = {United Kingdom},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}