8KB9
Structure of the WDR91 WD40 domain
Summary for 8KB9
| Entry DOI | 10.2210/pdb8kb9/pdb |
| Descriptor | WD repeat-containing protein 91 (2 entities in total) |
| Functional Keywords | effector, gtpase, wd40, endocytosis |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 39824.16 |
| Authors | Li, J.,Ma, X.L.,Banerjee, S.,Dong, Z.G. (deposition date: 2023-08-04, release date: 2024-08-07, Last modification date: 2024-12-18) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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