Crystallization of a newly discovered histidine acid phosphatase fromFrancisella tularensis
| Autor: | Richard L. Felts, John J. Tanner, Thomas J. Reilly, Michael J. Calcutt |
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| Rok vydání: | 2005 |
| Předmět: |
Male
Acid Phosphatase Phosphatase Biophysics Protein tyrosine phosphatase Crystallography X-Ray Biochemistry Legionella pneumophila Microbiology Bacterial Proteins Structural Biology Genetics Humans Histidine Francisella tularensis chemistry.chemical_classification biology Prostate Acid phosphatase Condensed Matter Physics biology.organism_classification Enzyme Prostatic acid phosphatase chemistry Crystallization Communications biology.protein Protein Tyrosine Phosphatases Crystallization |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:32-35 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309105039813 |
| Popis: | 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(1)2(1)2, with unit-cell parameters a = 61.96, c = 210.78 A. The asymmetric unit is predicted to contain one protein molecule, with a solvent content of 53%. A 1.75 A 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. |
| Databáze: | OpenAIRE |
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