2j68

From Proteopedia

Bacterial dynamin-like protein BDLP, GDP bound

PDB ID 2j68

Drag the structure with the mouse to rotate

Structural highlights

2j68 is a 1 chain structure with sequence from Nostoc punctiforme. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BDLP_NOSP7 Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangment, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bilayer; this does not stimulate subsequent GTPase activity. Does not bind lipids in the presence of GDP; perhaps GTP hydrolysis disrupts membrane-binding.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs). They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle division. Many bacteria are predicted by sequence to possess large GTPases with the same multidomain architecture that is found in DLPs. Mechanistic dissection of dynamin family members has been impeded by a lack of high-resolution structural data currently restricted to the GTPase and pleckstrin homology domains, and the dynamin-related human guanylate-binding protein. 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 FZL, 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 chloroplasts, questions the evolutionary origins of dynamins.

A bacterial dynamin-like protein.,Low HH, Lowe J Nature. 2006 Dec 7;444(7120):766-9. Epub 2006 Nov 22. PMID:17122778^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Low HH, Lowe J. A bacterial dynamin-like protein. Nature. 2006 Dec 7;444(7120):766-9. Epub 2006 Nov 22. PMID:17122778 doi:10.1038/nature05312
↑ Low HH, Lowe J. A bacterial dynamin-like protein. Nature. 2006 Dec 7;444(7120):766-9. Epub 2006 Nov 22. PMID:17122778 doi:10.1038/nature05312