X-RAY CRYSTALLOGRAPHIC STUDIES OF METAL TRAFFICKING PROTEINS AND METALLOENZYMES

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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. Beam time obtained from our previous proposal has led to the determination of structures of metal trafficking proteins and metalloenzymes. Structures of metal trafficking proteins include the copper chaperones Hah1 and CCS, the bacterial copper resistance protein PcoC, and the heterodimeric complex between the yeast ribonucleotide reductase Y2 and Y4 proteins. Enzyme structures include beta-lactam synthetase and mutants of ribonucleotide reductase R2. We propose to continue our studies of CCS, PcoC, Y2, Y4, and R2. In addition, we are pursuing the structure determination of CarA, which is related to beta-lactam synthetase. Finally, we have obtained diffracting crystals of particulate methane monooxygenase (pMMO), a membrane-bound enzyme that uses a catalytic copper center to oxidize methane to methanol, and plan to solve this structure by copper multiwavelength anomalous dispersion (MAD) phasing.