4UZZ

Crystal structure of the TtIFT52-46 complex

4UZZ の概要

• エントリーDOI: 10.2210/pdb4uzz/pdb
• 分子名称: INTRAFLAGELLAR TRANSPORT COMPLEX B PROTEIN 46 CARBOXY-TERMINAL PROTEIN, INTRAFLAGELLAR TRANSPORTER-LIKE PROTEIN (3 entities in total)
• 機能のキーワード: motor protein, cilium, ift, intracellular transport, flagellum
• 由来する生物種: TETRAHYMENA THERMOPHILA; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21172.83

構造登録者

Braeuer, P.,Taschner, M.,Lorentzen, E. (登録日: 2014-09-09, 公開日: 2014-11-05, 最終更新日: 2024-05-08)

主引用文献

Taschner, M.,Kotsis, F.,Braeuer, P.,Kuehn, E.W.,Lorentzen, E.
Crystal Structures of Ift70/52 and Ift52/46 Provide Insight Into Intraflagellar Transport B Core Complex Assembly.
J.Cell Biol., 207:269-, 2014

PubMed Abstract: Cilia are microtubule-based organelles that assemble via intraflagellar transport (IFT) and function as signaling hubs on eukaryotic cells. IFT relies on molecular motors and IFT complexes that mediate the contacts with ciliary cargo. To elucidate the architecture of the IFT-B complex, we reconstituted and purified the nonameric IFT-B core from Chlamydomonas reinhardtii and determined the crystal structures of C. reinhardtii IFT70/52 and Tetrahymena IFT52/46 subcomplexes. The 2.5-Å resolution IFT70/52 structure shows that IFT52330-370 is buried deeply within the IFT70 tetratricopeptide repeat superhelix. Furthermore, the polycystic kidney disease protein IFT88 binds IFT52281-329 in a complex that interacts directly with IFT70/IFT52330-381 in trans. The structure of IFT52C/IFT46C was solved at 2.3 Å resolution, and we show that it is essential for IFT-B core integrity by mediating interaction between IFT88/70/52/46 and IFT81/74/27/25/22 subcomplexes. Consistent with this, overexpression of mammalian IFT52C in MDCK cells is dominant-negative and causes IFT protein mislocalization and disrupted ciliogenesis. These data further rationalize several ciliogenesis phenotypes of IFT mutant strains.

PubMed: 25349261
DOI: 10.1083/JCB.201408002

実験手法

X-RAY DIFFRACTION (2.318 Å)