2j68

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{{Seed}}
 
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[[Image:2j68.png|left|200px]]
 
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==Bacterial dynamin-like protein BDLP, GDP bound==
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The line below this paragraph, containing "STRUCTURE_2j68", creates the "Structure Box" on the page.
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<StructureSection load='2j68' size='340' side='right'caption='[[2j68]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2j68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_punctiforme Nostoc punctiforme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J68 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
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{{STRUCTURE_2j68| PDB=2j68 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j68 OCA], [https://pdbe.org/2j68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j68 RCSB], [https://www.ebi.ac.uk/pdbsum/2j68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j68 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j6/2j68_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j68 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===BACTERIAL DYNAMIN-LIKE PROTEIN BDLP, GDP BOUND===
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A bacterial dynamin-like protein.,Low HH, Lowe J Nature. 2006 Dec 7;444(7120):766-9. Epub 2006 Nov 22. PMID:17122778<ref>PMID:17122778</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17122778}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2j68" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17122778 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17122778}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2J68 is a [[Single protein]] structure of 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=2J68 OCA].
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==Reference==
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A bacterial dynamin-like protein., Low HH, Lowe J, Nature. 2006 Dec 7;444(7120):766-9. Epub 2006 Nov 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17122778 17122778]
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[[Category: Nostoc punctiforme]]
[[Category: Nostoc punctiforme]]
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[[Category: Single protein]]
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[[Category: Low HH]]
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[[Category: Low, H H.]]
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[[Category: Lowe J]]
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[[Category: Lowe, J.]]
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[[Category: Dynamin]]
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[[Category: Fzl]]
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[[Category: Fzo]]
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[[Category: Gtpase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:22:51 2008''
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Current revision

Bacterial dynamin-like protein BDLP, GDP bound

PDB ID 2j68

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