<table><tr><td colspan='2'>[[2w6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nosp7 Nosp7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W6D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2w6d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_punctiforme_PCC_73102 Nostoc punctiforme PCC 73102]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6D FirstGlance]. <br>
[[http://www.uniprot.org/uniprot/BDLP_NOSP7 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.<ref>PMID:17122778</ref>
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[https://www.uniprot.org/uniprot/BDLP_NOSP7 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.<ref>PMID:17122778</ref>
2w6d is a 2 chain structure with sequence from Nostoc punctiforme PCC 73102. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Proteins of the dynamin superfamily mediate membrane fission, fusion, and restructuring events by polymerizing upon lipid bilayers and forcing regions of high curvature. In this work, we show the electron cryomicroscopy reconstruction of a bacterial dynamin-like protein (BDLP) helical filament decorating a lipid tube at approximately 11 A resolution. We fitted the BDLP crystal structure and produced a molecular model for the entire filament. The BDLP GTPase domain dimerizes and forms the tube surface, the GTPase effector domain (GED) mediates self-assembly, and the paddle region contacts the lipids and promotes curvature. Association of BDLP with GMPPNP and lipid induces radical, large-scale conformational changes affecting polymerization. Nucleotide hydrolysis seems therefore to be coupled to polymer disassembly and dissociation from lipid, rather than membrane restructuring. Observed structural similarities with rat dynamin 1 suggest that our results have broad implication for other dynamin family members.
Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving.,Low HH, Sachse C, Amos LA, Lowe J Cell. 2009 Dec 24;139(7):1342-52. PMID:20064379[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, Sachse C, Amos LA, Lowe J. Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. Cell. 2009 Dec 24;139(7):1342-52. PMID:20064379 doi:10.1016/j.cell.2009.11.003
