CRYSTAL STRUCTURE OF NON-RIBOSOMAL PEPTIDE SYNTHETASES AND RELATED PROTEINS

非核糖体肽合成酶及相关蛋白的晶体结构

• 批准号: 7357735
• 负责人: ANDREW M GULICK
• 金额: $ 3.05万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-07-01 至 2007-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7357735
• 关键词: CRYSTAL; STRUCTURE; NON; RIBOSOMAL; PEPTIDE

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 Non-Ribosomal Peptide Synthetases are modular, multidomain enzymes that synthesize peptides that frequently show antibiotic activity. These enzymes have multiple catalytic domains joined in an assembly line to catalyze the sequential elongation of the peptide product. We are interested in studying these proteins structurally to provide clues to how these distinct catalytic domains interact. Our studies are focused on the NRPS adenylation domains that bind to amino acids and covalently attach them to a pantetheine cofactor of an NRPS carrier protein domain. We wish to collect --higher resolution data to obtain a better model for the EntB protein --MAD data for the HBAL structure determination --high resolution data on several mutant enzymes of the CBAL to test the Domain Alternation hypothesis.

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。非核糖体肽合成酶是模块化的，多结构域的酶，合成肽，经常显示抗生素活性。这些酶具有多个催化结构域，连接在一条装配线上，催化肽产物的顺序延伸。我们感兴趣的是研究这些蛋白质的结构，为这些不同的催化结构域如何相互作用提供线索。我们的研究主要集中在NRPS腺苷化结构域，该结构域与氨基酸结合，并将其共价连接到NRPS载体蛋白结构域的泛茶氨酸辅因子上。我们希望收集更高分辨率的数据，以获得更好的enb蛋白模型；收集MAD数据，以确定HBAL结构；收集CBAL几种突变酶的高分辨率数据，以检验结构域交替假说。