STRUCTURE OF PROLYL-4-HYDROXYLASE FROM BACILLUS ANTHRACIS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Collagen prolyl-4-hydroxylase (P4H) is an essential enzyme in collagen biosynthesis and disruption of P4H function is known to contribute to fibrotic diseases. The only structure available is a 100 amino acid fragment of the human enzyme consisting of the substrate binding domain (out of 517 amino acids total). No structures currently exist that include the catalytic domain responsible for binding both iron and alpha-ketoglutarate. Our crystals contain the full-length Bacillus anthracis and are expected to elucidate the mechanism of activity. We have collected a complete data set using a home source for P4H. Since this is a novel structure with no similar structures known, molecular replacement is not an option for structure determination.