A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis

摘要

Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI_RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 angstrom resolution. The SIP crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 48.04, b = 78.31, c = 67.71 angstrom, alpha = 90, beta = 99.94, gamma = 90 degrees, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined similar to 2 angstrom resolution SIP structures with similar to 30% sequence identity as templates are ongoing.