5HAS

Crystal structure of the N-terminal DCB-HUS domain of T. terrestris Sec7

5HAS の概要

• エントリーDOI: 10.2210/pdb5has/pdb
• 分子名称: Sec7 (2 entities in total)
• 機能のキーワード: armadillo, arf-gef, tgn, transport, protein transport
• 由来する生物種: Thielavia terrestris
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 207572.28

構造登録者

Richardson, B.C.,Fromme, J.C. (登録日: 2015-12-30, 公開日: 2016-01-27, 最終更新日: 2024-03-06)

主引用文献

Richardson, B.C.,Halaby, S.L.,Gustafson, M.A.,Fromme, J.C.
The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.
Elife, 5:-, 2016

PubMed Abstract: The Golgi complex is the central sorting compartment of eukaryotic cells. Arf guanine nucleotide exchange factors (Arf-GEFs) regulate virtually all traffic through the Golgi by activating Arf GTPase trafficking pathways. The Golgi Arf-GEFs contain multiple autoregulatory domains, but the precise mechanisms underlying their function remain largely undefined. We report a crystal structure revealing that the N-terminal DCB and HUS regulatory domains of the Arf-GEF Sec7 form a single structural unit. We demonstrate that the established role of the N-terminal region in dimerization is not conserved; instead, a C-terminal autoinhibitory domain is responsible for dimerization of Sec7. We find that the DCB/HUS domain amplifies the ability of Sec7 to activate Arf1 on the membrane surface by facilitating membrane insertion of the Arf1 amphipathic helix. This enhancing function of the Sec7 N-terminal domains is consistent with the high rate of Arf1-dependent trafficking to the plasma membrane necessary for maximal cell growth.

PubMed: 26765562
DOI: 10.7554/eLife.12411

実験手法

X-RAY DIFFRACTION (2.653 Å)