X-RAY CRYSTALLOGRAPHIC STUDIES OF METAL TRAFFICKING PROTEINS AND METALLOENZYMES

金属运输蛋白和金属酶的 X 射线晶体学研究

• 批准号: 7370361
• 负责人: AMY C. ROSENZWEIG
• 金额: $ 0.3万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370361
• 关键词: RAY; CRYSTALLOGRAPHIC; STUDIES; METAL; TRAFFICKING

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.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。从我们以前的建议获得的束时间导致金属运输蛋白质和金属酶的结构的确定。金属转运蛋白的结构包括铜分子伴侣Hah 1和CCS、细菌铜抗性蛋白PcoC以及酵母核糖核苷酸还原酶Y2和Y 4蛋白之间的异二聚体复合物。酶结构包括β-内酰胺合成酶和核糖核苷酸还原酶R2的突变体。我们建议继续研究CCS、PcoC、Y2、Y 4和R2。此外，我们正在进行与β-内酰胺合成酶相关的CarA的结构测定。最后，我们已经获得了颗粒甲烷单加氧酶（pMMO）的衍射晶体，这是一种膜结合酶，它使用催化铜中心将甲烷氧化为甲醇，并计划通过铜多波长异常色散（MAD）定相来解决这种结构。