7QLA
Structure of the Rab GEF complex Mon1-Ccz1
Summary for 7QLA
| Entry DOI | 10.2210/pdb7qla/pdb |
| EMDB information | 14066 |
| Descriptor | Vacuolar fusion protein MON1, Ccz1 (2 entities in total) |
| Functional Keywords | guanine nucleotide exchange factor, tld rab gef, longin domains, pip binding, endocytosis |
| Biological source | Chaetomium thermophilum More |
| Total number of polymer chains | 2 |
| Total formula weight | 133352.29 |
| Authors | Klink, B.U.,Herrmann, E.,Antoni, C.,Langemeyer, L.,Kiontke, S.,Gatsogiannis, C.,Ungermann, C.,Raunser, S.,Kuemmel, D. (deposition date: 2021-12-20, release date: 2022-02-09, Last modification date: 2025-07-09) |
| Primary citation | Klink, B.U.,Herrmann, E.,Antoni, C.,Langemeyer, L.,Kiontke, S.,Gatsogiannis, C.,Ungermann, C.,Raunser, S.,Kummel, D. Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation. Proc.Natl.Acad.Sci.USA, 119:-, 2022 Cited by PubMed Abstract: Activation of the GTPase Rab7/Ypt7 by its cognate guanine nucleotide exchange factor (GEF) Mon1-Ccz1 marks organelles such as endosomes and autophagosomes for fusion with lysosomes/vacuoles and degradation of their content. Here, we present a high-resolution cryogenic electron microscopy structure of the Mon1-Ccz1 complex that reveals its architecture in atomic detail. Mon1 and Ccz1 are arranged side by side in a pseudo-twofold symmetrical heterodimer. The three Longin domains of each Mon1 and Ccz1 are triangularly arranged, providing a strong scaffold for the catalytic center of the GEF. At the opposite side of the Ypt7-binding site, a positively charged and relatively flat patch stretches the Longin domains 2/3 of Mon1 and functions as a phosphatidylinositol phosphate-binding site, explaining how the GEF is targeted to membranes. Our work provides molecular insight into the mechanisms of endosomal Rab activation and serves as a blueprint for understanding the function of members of the Tri Longin domain Rab-GEF family. PubMed: 35105815DOI: 10.1073/pnas.2121494119 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.85 Å) |
Structure validation
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