1VG9

The crystal structures of the REP-1 protein in complex with C-terminally truncated Rab7 protein

1VG9 の概要

• エントリーDOI: 10.2210/pdb1vg9/pdb
• 関連するPDBエントリー: 1LTX 1VG0 1VG1 1VG8
• 分子名称: Rab proteins geranylgeranyltransferase component A 1, Ras-related protein Rab-7, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: rab prenylation, post-translational modification, protein binding-protein transport complex, protein binding/protein transport
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cytoplasm, cytosol : P37727; Cytoplasmic vesicle, phagosome membrane ; Peripheral membrane protein ; Cytoplasmic side : P09527
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 378304.88

構造登録者

Rak, A.,Pylypenko, O.,Niculae, A.,Pyatkov, K.,Goody, R.S.,Alexandrov, K. (登録日: 2004-04-23, 公開日: 2004-07-20, 最終更新日: 2023-10-25)

主引用文献

Rak, A.,Pylypenko, O.,Niculae, A.,Pyatkov, K.,Goody, R.S.,Alexandrov, K.
Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease
Cell(Cambridge,Mass.), 117:749-760, 2004

PubMed Abstract: Members of the RabGDI/REP family serve as multifunctional regulators of the Rab family of GTP binding proteins. Mutations in members of this family, such as REP-1, lead to abnormalities, including progressive retinal degradation (choroideremia) in humans. The crystal structures of the REP-1 protein in complex with monoprenylated or C-terminally truncated Rab7 proteins revealed that Rab7 interacts with the Rab binding platform of REP-1 via an extended interface involving the Switch 1 and 2 regions. The C terminus of the REP-1 molecule functions as a mobile lid covering a conserved hydrophobic patch on the surface of REP-1 that in the complex coordinates the C terminus of Rab proteins. Using semisynthetic fluorescent Rab27A, we demonstrate that although Rab27A can be prenylated by REP-2, this reaction can be effectively inhibited by other Rab proteins, providing a possible explanation for the accumulation of unprenylated Rab27A in choroideremia.

PubMed: 15186776
DOI: 10.1016/j.cell.2004.05.017

実験手法

X-RAY DIFFRACTION (2.5 Å)