4P17

Crystal structure of the Chlamydomonas flagellar RabGAP TBC domain.

4P17 の概要

• エントリーDOI: 10.2210/pdb4p17/pdb
• 分子名称: RabGAP/TBC protein (2 entities in total)
• 機能のキーワード: flagella, tbc, rabgap, chlamydomonas, cilia, unknown function
• 由来する生物種: Chlamydomonas reinhardtii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71349.88

構造登録者

Bhogaraju, S.,Lorentzen, E. (登録日: 2014-02-25, 公開日: 2014-04-30, 最終更新日: 2023-12-27)

主引用文献

Bhogaraju, S.,Lorentzen, E.
Crystal structure of a Chlamydomonas reinhardtii flagellar RabGAP TBC-domain at 1.8 angstrom resolution.
Proteins, 82:2282-2287, 2014

PubMed Abstract: Rab GTPases play a crucial role in the regulation of many intracellular membrane trafficking pathways including endocytosis and ciliogenesis. Rab GTPase activating proteins (RabGAPs) increase the GTP hydrolysis rate of Rab GTPases and turn them into guanine nucleotide diphosphate (GDP) bound inactive form. Here, we determined the crystal structure of the putative catalytic domain of a RabGAP (which we name CrfRabGAP) that is found in the flagellar proteome of the unicellular green alga Chlamydomonas reinhardtii. BLAST searches revealed potential human orthologues of CrfRabGAP as TBC1D3 and TBC1D26. Sequence and structural comparison with other canonical RabGAPs revealed that the CrfRabGAP does not contain the canonical catalytic residues required for the activation of Rab GTPases. The function of noncanonical RabGAPs-like CrfRabGAP might be to serve as Rab effectors rather than activators.

PubMed: 24810373
DOI: 10.1002/prot.24597

実験手法

X-RAY DIFFRACTION (1.7941 Å)