東京大学 · Biochemistry, Genetics and Molecular Biology
오오사무 누레키 교수의 연구실은 생물막의 기능과 구조를 해부하는 데 초점을 맞추고 있습니다. 주로 세포 간 접합 구조인 타이트 점액과 펌프 단백질인 P4-ATPase의 고해상도 구조를 규명함으로써 세포막의 지질 비대칭성과 물질 통과 조절 메커니즘을 밝혀내고 있습니다. 특히, 단백질의 3차 구조와 기능적 동역학을 결합한 고해상도 구조 생물학적 접근을 통해 생물학적 막의 기초 메커니즘을 규명하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
Tight junctions are cell-cell adhesion structures in epithelial cell sheets that surround organ compartments in multicellular organisms and regulate the permeation of ions through the intercellular space. Claudins are the major constituents of tight junctions and form strands that mediate cell adhesion and function as paracellular barriers. We report the structure of mammalian claudin-15 at a resolution of 2.4 angstroms. The structure reveals a characteristic β-sheet fold comprising two extracel
High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the valyl
In eukaryotic membranes, type IV P-type adenosine triphosphatases (P4-ATPases) mediate the translocation of phospholipids from the outer to the inner leaflet and maintain lipid asymmetry, which is critical for membrane trafficking and signaling pathways. Here, we report the cryo-electron microscopy structures of six distinct intermediates of the human ATP8A1-CDC50a heterocomplex at resolutions of 2.6 to 3.3 angstroms, elucidating the lipid translocation cycle of this P4-ATPase. ATP-dependent pho
