STUDIES OF METALLOPROTEINS (PFL ACTIVATING ENZYME, HPPE, NIKR, SYRB2)

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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. Metals and metalloproteins are essential for many cellular processes. Our laboratory uses macromolecular crystallography to study the structure and function of metalloproteins. These proteins include nickel regulatory protein NikR, a DNA-binding protein; pyruvate-formate lyase activating enzyme (PFL-AE), a Radical SAM enzyme involved in anaerobic metabolism by formation of a protein bound glycyl radical on pyruvate formate lyase; hydroxypropylphosphonic acid epoxidase (HppE), which uses a mononuclear iron site to catalyze a unique epoxidation; and SyrB2, a mononuclear iron protein involved in natural product biosynthesis.