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2w6d

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Revision as of 20:48, 24 December 2014

BACTERIAL DYNAMIN-LIKE PROTEIN LIPID TUBE BOUND

Structural highlights

2w6d is a 2 chain structure with sequence from Nostoc punctiforme. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2j69, 2j68
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[B2IZD3_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

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w6d"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2w6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_punctiforme Nostoc punctiforme]. 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>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CPL:1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>CPL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CPL:1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>CPL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j69|2j69]], [[2j68|2j68]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j69|2j69]], [[2j68|2j68]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6d RCSB], [http://www.ebi.ac.uk/pdbsum/2w6d PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6d RCSB], [http://www.ebi.ac.uk/pdbsum/2w6d PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/B2IZD3_NOSP7 B2IZD3_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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 </StructureSection>
 [[Category: Nostoc punctiforme]]
-[[Category: Amos, L A.]]
+[[Category: Amos, L A]]
-[[Category: Low, H H.]]
+[[Category: Low, H H]]
-[[Category: Lowe, J.]]
+[[Category: Lowe, J]]
-[[Category: Sachse, C.]]
+[[Category: Sachse, C]]
 [[Category: Dynamin]]
 [[Category: Gtpase]]

2w6d

From Proteopedia

Revision as of 20:48, 24 December 2014

BACTERIAL DYNAMIN-LIKE PROTEIN LIPID TUBE BOUND

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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