U.S.-Czech Biomolecular Research on Structural Studies of a Novel Flavodoxin-like Protein

美国的目标是-捷克普林斯顿大学的Jannette Carey和南波希米亚大学的IbergSmatanova之间的研究项目，Ceske Budejovice，是为了扩展我们对一类重要蛋白质的结构和分子功能之间关系的知识，并将这些特征与它们的生物学作用联系起来。 该项目特别涉及蛋白质BABA的结构研究，该蛋白质可以弱结合黄素单核苷酸（FMN）。该蛋白存在于多种细菌和真核生物中，属于一个保守的多聚体类黄素氧还蛋白家族。研究人员已经获得了apo-AubA的衍射质量晶体。 这种蛋白质的兴趣源于计算机建模和生化实验的结果，建立有趣的差异相比，同源flavodoxins，并建议参与氧化应激反应。 由美国和捷克的高级和初级生物化学家组成的团队计划：1）从结构上表征野生型蛋白质，2）表征子域改组产物。 结果预计将提供三维的见解的建筑安排的辅因子结合，二聚化，和功能结构域。 成功将提高我们的黄素和DNA结合域如何结合在一个单一的多肽的知识，通过定点诱变指导未来的蛋白质工程的影响。该项目在生物学和物理科学的接口实现了通过使美国和中欧的专家能够联合收割机互补人才和共享研究资源，在强烈的共同利益和能力领域推进科学知识的计划目标。 更广泛的影响包括通过在合作机构工作和直接参与先进的结构生物学，包括建模技术和X射线衍射分析，将美国和捷克学生介绍给国际研究界。 该项目由分子和细胞生物科学部的生物分子系统集群和NSF国际科学与工程办公室联合资助。

The goal of this U.S.-Czech research project between Jannette Carey of Princeton University and Ivana Smatanova of the University of South Bohemia, Ceske Budejovice, is to extend our knowledge of the relationships between structure and molecular functions in an important class of proteins and to relate these features to their biological roles. The project specifically involves the structural investigation of the protein WrbA, which can weakly bind flavin mononucleotide (FMN). This protein is found in diverse bacteria and eukaryotes and belongs to a conserved family of novel multimeric flavodoxin-like proteins. The researchers have obtained diffraction-quality crystals of the apo-WrbA. Interest in this protein stems from available results from computer modeling and biochemical experiments that establish interesting differences when compared with homologous flavodoxins and suggest involvement in oxidative-stress responses. The team of senior and junior U.S. and Czech biochemists plans to: 1) structurally characterize the wild type protein and 2) characterize subdomain-shuffling products. Results are expected to provide three-dimensional insights into the architectural arrangement of the cofactor binding, dimerization, and functional domains. Success would enhance our knowledge of how flavin and DNA binding domains are combined in a single polypeptide, with implications for guiding future protein engineering through site-directed mutagenesis. This project at the interface of biology and physical sciences fulfills the program objective of advancing scientific knowledge by enabling experts in the United States and Central Europe to combine complementary talents and share research resources in areas of strong mutual interest and competence. Broader implications include the introduction of U.S. and Czech students to the international research community through work at partner institutions and direct involvement in advanced structural biology, including modeling techniques and x-ray diffraction analysis. The project is funded jointly by the Biomolecular Systems Cluster in the Division of Molecular and Cellular Biosciences and the Office of International Science and Engineering at NSF.