STRUCTURAL BIOLOGY OF MACROMOLECULAR STRUCTURE

大分子结构的结构生物学

• 批准号: 3770004
• 负责人: A C STEVEN
• 金额: --
• 依托单位: NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3770004
• 关键词: Alphaherpesvirinae; Bordetella pertussis; adhesin; capsid; conformation; electron microscopy; image processing; immunoelectron microscopy; macromolecule; microorganism hemagglutinin; protein folding; protein structure function; scanning electron microscopy; structural biology; virus protein

This Laboratory seeks to elucidate the mechanisms that govern the assembly of supramolecular complexes and the folding of macromolecules, as well as those that underlie the synthesis of viruses, organelles, and other high order structures. In the past year, we have discovered a radical departure from equivalence in the packing of protein molecules in the capsid of bacteriophage HK97. The same protein forms both the hexons and pentons, but whereas the pentons are cyclically symmetric pentamers, the hexons are not cyclically symmetric, but consist of two apposed trimers with a mutual lateral displacement of at least 20 Angstroms. In herpes simplex virus, we have localized the small abundant capsid protein, VP26 (12 Kda) to the outer tips of hexons by quantitative difference imaging. Its exposed location suggests that its role may lie in coupling the capsid to the surrounding tegument. We have also studied several of the major molecules displayed at the outer surface of the pathogenic bacterium, Bordetella pertussis. One of these, filamentous hemagglutinin, is a high immunogenic adhesion. FHA was found to assume a novel 50nm-long monomeric hairpin structure. Its sequence contains two protracted runs of 19-residue repeats which strongly resemble the leucine-rich repeats (LRRs) that are present in a set of eukaryotic proteins, many of which have been implicated in intercellular adhesion phenomena. This observation suggests that FHA repeats may be involved in the adhesion of B. pertussis cells to the respiratory tract.

本实验室旨在阐明控制 超分子复合物的组装和大分子的折叠， 以及那些构成病毒、细胞器和 其他高级结构。 在过去的一年里，我们发现了一个 在蛋白质分子的堆积中， 在噬菌体HK97的衣壳中。 相同的蛋白质形成了 六子和五子，但是五子是循环对称的， 五聚体，六邻体不是循环对称的，而是由两个 相互横向位移至少为20 愤怒。 在单纯疱疹病毒中， 衣壳蛋白，VP26（12 Kda）的外尖端的六邻体通过定量 差分成像 它暴露的位置表明它的作用可能在于 将衣壳与周围的皮层结合起来 我们还研究了 几个主要分子显示在外表面的 致病菌，百日咳杆菌。 其中一种是丝状的 血凝素是一种高免疫原性粘附。 FHA被发现假设 一种新颖的50 nm长的单体发夹结构。 它的序列包含两个 长时间的19个残基重复序列， 富含亮氨酸的重复序列（LRR）存在于一组真核生物中， 蛋白质，其中许多与细胞间粘附有关 现象。 这一观察结果表明，FHA重复可能参与 在B的粘附中。百日咳细胞进入呼吸道。