Open AccessCrystallization of a newly discovered histidine acid phosphatase from Francisella tularensis
Author(s) -
Felts Richard L.,
Reilly Thomas J.,
Calcutt Michael J.,
Tanner John J.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105039813
Subject(s) - histidine , acid phosphatase , francisella tularensis , phosphatase , crystallization , legionella pneumophila , molecular replacement , amino acid , peptide sequence , biology , biochemistry , chemistry , crystallography , bacteria , enzyme , genetics , virulence , organic chemistry , gene
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 P 4 1 2 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.