3BBP

Rab6-GTP:GCC185 Rab binding domain complex

3BBP の概要

• エントリーDOI: 10.2210/pdb3bbp/pdb
• 関連するPDBエントリー: 2GIL
• 分子名称: Ras-related protein Rab-6A, GRIP and coiled-coil domain-containing protein 2, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: golgi complex; grip domain; rab gtpase; arl gtpase; golgin; rab effector; clasp protein, acetylation, alternative splicing, er-golgi transport, golgi apparatus, gtp-binding, lipoprotein, membrane, methylation, nucleotide-binding, phosphorylation, prenylation, protein transport, transport, coiled coil, cytoplasm, polymorphism, protein transport-splicing complex, protein transport/splicing
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Golgi apparatus membrane; Lipid-anchor: P20340; Cytoplasm: Q8IWJ2
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 97661.58

構造登録者

Schweizer Burguete, A.,Fenn, T.D.,Brunger, A.T.,Pfeffer, S.R. (登録日: 2007-11-09, 公開日: 2008-02-05, 最終更新日: 2023-08-30)

主引用文献

Burguete, A.S.,Fenn, T.D.,Brunger, A.T.,Pfeffer, S.R.
Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.
Cell(Cambridge,Mass.), 132:286-298, 2008

PubMed Abstract: GCC185 is a large coiled-coil protein at the trans Golgi network that is required for receipt of transport vesicles inbound from late endosomes and for anchoring noncentrosomal microtubules that emanate from the Golgi. Here, we demonstrate that recruitment of GCC185 to the Golgi is mediated by two Golgi-localized small GTPases of the Rab and Arl families. GCC185 binds Rab6, and mutation of residues needed for Rab binding abolishes Golgi localization. The crystal structure of Rab6 bound to the GCC185 Rab-binding domain reveals that Rab6 recognizes a two-fold symmetric surface on a coiled coil immediately adjacent to a C-terminal GRIP domain. Unexpectedly, Rab6 binding promotes association of Arl1 with the GRIP domain. We present a structure-derived model for dual GTPase membrane attachment that highlights the potential ability of Rab GTPases to reach binding partners at a significant distance from the membrane via their unstructured and membrane-anchored, hypervariable domains.

PubMed: 18243103
DOI: 10.1016/j.cell.2007.11.048

実験手法

X-RAY DIFFRACTION (3 Å)