4V0N

Crystal structure of BBS1N in complex with ARL6DN, soaked with mercury

4V0N の概要

• エントリーDOI: 10.2210/pdb4v0n/pdb
• 関連するPDBエントリー: 4V0K 4V0M 4V0O
• 分子名称: ARF-LIKE SMALL GTPASE, BARDET-BIEDL SYNDROME 1 PROTEIN, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: hydrolase-structural protein complex, bbsome, gtp, coat complex, hydrolase/structural protein
• 由来する生物種: CHLAMYDOMONAS REINHARDTII; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 274322.40

構造登録者

Mourao, A.,Lorentzen, E. (登録日: 2014-09-17, 公開日: 2014-11-19, 最終更新日: 2024-11-20)

主引用文献

Mourao, A.,Nager, A.R.,Nachury, M.V.,Lorentzen, E.
Structural Basis for Membrane Targeting of the Bbsome by Arl6
Nat.Struct.Mol.Biol., 21:1035-, 2014

PubMed Abstract: The BBSome is a coat-like ciliary trafficking complex composed of proteins mutated in Bardet-Biedl syndrome (BBS). A critical step in BBSome-mediated sorting is recruitment of the BBSome to membranes by the GTP-bound Arf-like GTPase ARL6. We have determined crystal structures of Chlamydomonas reinhardtii ARL6-GDP, ARL6-GTP and the ARL6-GTP-BBS1 complex. The structures demonstrate how ARL6-GTP binds the BBS1 β-propeller at blades 1 and 7 and explain why GTP- but not GDP-bound ARL6 can recruit the BBSome to membranes. Single point mutations in the ARL6-GTP-BBS1 interface abolish the interaction of ARL6 with the BBSome and prevent the import of BBSomes into cilia. Furthermore, we show that BBS1 with the M390R mutation, responsible for 30% of all reported BBS disease cases, fails to interact with ARL6-GTP, thus providing a molecular rationale for patient pathologies.

PubMed: 25402481
DOI: 10.1038/NSMB.2920

実験手法

X-RAY DIFFRACTION (3.131 Å)