The crystal structure of dynamin

Article

关键词: PLECKSTRIN HOMOLOGY DOMAIN;    CLATHRIN-MEDIATED ENDOCYTOSIS;    GTPASE ACTIVITY;    IN-VIVO;    CONFORMATIONAL-CHANGES;    BINDING PROTEINS;    MECHANISM;    FISSION;    MITOCHONDRIAL;    CONSTRICTION;   

DOI  :  10.1038/nature10441

来源: SCIE

【 摘 要 】

Dynamin-related proteins (DRPs) are multi-domain GTPases that function via oligomerization and GTP-dependent conformational changes to play central roles in regulating membrane structure across phylogenetic kingdoms. How DRPs harness self-assembly and GTP-dependent conformational changes to remodel membranes is not understood. Here we present the crystal structure of an assembly-deficient mammalian endocytic DRP, dynamin 1, lacking the proline-rich domain, in its nucleotide-free state. The dynamin 1 monomer is an extended structure with the GTPase domain and bundle signalling element positioned on top of a long helical stalk with the pleckstrin homology domain flexibly attached on its opposing end. Dynamin 1 dimer and higher order dimer multimers form via interfaces located in the stalk. Analysis of these interfaces provides insight into DRP family member specificity and regulation and provides a framework for understanding the biogenesis of higher order DRP structures and the mechanism of DRP-mediated membrane scission events.

【 授权许可】

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