8KB9
Structure of the WDR91 WD40 domain
8KB9 の概要
エントリーDOI | 10.2210/pdb8kb9/pdb |
分子名称 | WD repeat-containing protein 91 (2 entities in total) |
機能のキーワード | effector, gtpase, wd40, endocytosis |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 39824.16 |
構造登録者 | |
主引用文献 | Ma, X.,Li, J.,Liu, N.,Banerjee, S.,Hu, X.,Wang, X.,Dong, J.,Liu, K.,Yang, C.,Dong, Z. Insights into the distinct membrane targeting mechanisms of WDR91 family proteins. Structure, 32:2287-2300.e4, 2024 Cited by PubMed Abstract: WDR91 and SORF1, members of the WD repeat-containing protein 91 family, control phosphoinositide conversion by inhibiting phosphatidylinositol 3-kinase activity on endosomes, which promotes endosome maturation. Here, we report the crystal structure of the human WDR91 WD40 domain complexed with Rab7 that has an unusual interface at the C-terminus of the Rab7 switch II region. WDR91 is highly selective for Rab7 among the tested GTPases. A LIS1 homology (LisH) motif within the WDR91 N-terminal domain (NTD) mediates self-association and may contribute partly to the augmented interaction between full-length WDR91 and Rab7. Both the Rab7 binding site and the LisH motif are indispensable for WDR91 function in endocytic trafficking. For the WDR91 orthologue SORF1 lacking the C-terminal WD40 domain, a C-terminal amphipathic helix (AH) mediates strong interactions with liposomes containing acidic lipids. During evolution the human WDR91 ancestor gene might have acquired a WD40 domain to replace the AH for endosomal membrane targeting. PubMed: 39426373DOI: 10.1016/j.str.2024.09.023 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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