ROGER KORNBERG PRT TIME

罗杰·科恩伯格 PRT 时间

• 批准号: 7954170
• 负责人: ROGER D KORNBERG
• 金额: $ 1.59万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-03-01 至 2010-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7954170
• 关键词: Achievement; Amanitins; Binding; Biochemical; Collection; Complex; Computer Retrieval of Information on Scientific Projects Database; DNA; DNA Polymerase II; Electrons; Enzymes; Funding; Goals; Grant; Hand; Institution; Nucleic Acids; Phase; Polymerase; Proteins; RNA; RNA Polymerase II; Research; Research Personnel; Resolution; Resources; Solutions; Source; Structure; Time; Transcription Factor TFIIB; United States National Institutes of Health; X-Ray Crystallography; dalton; inhibitor/antagonist; novel; outcome forecast; polypeptide; structural biology; synchrotron radiation; transcription factor TFIIE

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 goal of the proposed research is to determine the x-ray structures of RNA polymerase II and of its complexes with nucleic acids and auxiliary protein factors at atomic resolution. The problem is challenging, since the polymerase alone comprises 15 polypeptides with a total mass of nearly 600,000 Dalton, and addition of the auxiliary factors doubles both the number of polypeptides and the protein mass. Solution of the problem requires a combination of biochemical studies, electron and X-ray crystallography. Eight types of RNA polymerase II crystal are now in hand, crystals of the native enzyme, and cocrystals with DNA, with RNA, with both DNA and RNA in the transcriptionally active state, with TFIIB, with TFIIE, with the additional polymerase subunits RPB4 and RPB7, and with the tight-binding inhibitor a-amanitin. Recent progress includes a low resolution envelope and phases to 6.5 ¿, and the recent collection of several novel heavy atom cluster complexed with RNA Pol II. The prognosis is now very good for the rapid achievement of a high resolution structure.

该副本是使用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这是调查员的机构。 拟议的研究的目的是确定原子分辨率下的RNA聚合酶II及其与核酸和辅助蛋白质因子的复合物的X射线结构。该问题受到挑战，因为单独的聚合酶包含15种多肽，总质量为近60万道尔顿，而辅助因子的添加使多肽的数量和蛋白质质量增加了一倍。问题解决方案需要生化研究，电子和X射线晶体学的结合。 Eight types of RNA polymerase II crystal are now in hand, crystals of the native enzyme, and cocrystals with DNA, with RNA, with both DNA and RNA in the transcriptionally active state, with TFIIB, with TFIIE, with the additional polymerase subunits RPB4 and RPB7, and with the tight-binding inhibitor a-amanitin.最近的进展包括低分辨率的包膜和6.5€的相位，以及最近与RNA Pol II复合的几个新型重原子聚类的集合。现在，预后非常适合快速实现高分辨率结构。