X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN A

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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. The haloacid dehalogenase (HAD) superfamily is comprised of structurally homologous enzymes that share several conserved sequence motifs in their active site. The major function of HAD members are phsophohydrolysis. HAD superfamily members can be classified to 3 subfamilies: type I, type II and type III depending on domain organization.In type I and type II members, a mobile cap domain reorients upon substrate binding, closing the active site to bujk solvent. The type III members lack this addition domain. My research has focused on understanding the function of several putative phosphatases in different bacteria. Protein RifM is a key enzyme in the synthatic pathway of AHBA, which is the precusor of natural antibiotic rifamycin. RifM belongs to HAD type I subfamily. Until now, the detailed function of RifM is still unclear. My goal is to solve RifM native and liganed structures and thus reveal its physioligical function in the synthatic pathway of AHBA.