期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 66, 期 -, 页码 26-28出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109047599
关键词
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资金
- Cystic Fibrosis Foundation [MADDEN08G0, STANTO97R0]
- NIH [R01-DK075309, T32-AI007519, T32-DK007301]
- Rosalind Borison Memorial Predoctoral Fellowship
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [T32AI007519] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK075309] Funding Source: NIH RePORTER
The opportunistic pathogen Pseudomonas aeruginosa secretes a protein that triggers the accelerated degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) in airway epithelial cells. This protein, which is known as the CFTR inhibitory factor ( Cif), acts as a virulence factor and may facilitate airway colonization by P. aeruginosa. Based on sequence similarity Cif appears to be an epoxide hydrolase ( EH), but it lacks several of the conserved features found in the active sites of canonical members of the EH family. Here, the crystallization of purified recombinant Cif by vapor diffusion is reported. The crystals formed in space group C2, with unit-cell parameters a = 167.4, b = 83.6, c = 88.3 angstrom, beta = 100.6 degrees. The crystals diffracted to 2.39 angstrom resolution on a rotating-anode source. Based on the calculated Matthews coefficient (2.2 angstrom(3) Da(-1)), it appears that the asymmetric unit contains four molecules.
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