1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

Correspondence to: Jan Löwe¹ Correspondence and requests for materials should be addressed to J.L. (Email: jyl@mrc-lmb.cam.ac.uk). Atomic coordinates produced in this study have been deposited in the Protein Data Bank under accession codes 2J69 (BDLP) and 2J68 (BDLP-GDP).

Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs)¹. They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle division¹. Many bacteria are predicted by sequence to possess large GTPases with the same multidomain architecture that is found in DLPs². Mechanistic dissection of dynamin family members has been impeded by a lack of high-resolution structural data currently restricted to the GTPase^{3, 4} and pleckstrin homology⁵ domains, and the dynamin-related human guanylate-binding protein⁶. Here we present the crystal structure of a cyanobacterial DLP in both nucleotide-free and GDP-associated conformation. The bacterial DLP shows dynamin-like qualities, such as helical self-assembly and tubulation of a lipid bilayer. In vivo, it localizes to the membrane in a manner reminiscent of FZL⁷, a chloroplast-specific dynamin-related protein with which it shares sequence similarity. Our results provide structural and mechanistic insight that may be relevant across the dynamin superfamily. Concurrently, we show compelling similarity between a cyanobacterial and chloroplast DLP that, given the endosymbiotic ancestry of chloroplasts⁸, questions the evolutionary origins of dynamins.

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