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2x2f

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[[Image:2x2f.png|left|200px]]
 
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==Dynamin 1 GTPase dimer, short axis form==
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The line below this paragraph, containing "STRUCTURE_2x2f", creates the "Structure Box" on the page.
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<StructureSection load='2x2f' size='340' side='right'caption='[[2x2f]], [[Resolution|resolution]] 2.00&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'>[[2x2f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2F FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_2x2f| PDB=2x2f | 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=2x2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2f OCA], [https://pdbe.org/2x2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x2f RCSB], [https://www.ebi.ac.uk/pdbsum/2x2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x2f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DYN1_HUMAN DYN1_HUMAN] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x2/2x2f_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=2x2f 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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Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin's basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-).The structure reveals dynamin's catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase-GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission.
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===DYNAMIN 1 GTPASE DIMER, SHORT AXIS FORM===
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G domain dimerization controls dynamin's assembly-stimulated GTPase activity.,Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F Nature. 2010 May 27;465(7297):435-40. Epub 2010 Apr 28. PMID:20428113<ref>PMID:20428113</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_20428113}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2x2f" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20428113 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20428113}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2x2f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2F OCA].
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==Reference==
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<ref group="xtra">PMID:020428113</ref><references group="xtra"/>
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[[Category: Dynamin GTPase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Acharya, S.]]
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[[Category: Large Structures]]
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[[Category: Chappie, J S.]]
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[[Category: Acharya S]]
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[[Category: Dyda, F.]]
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[[Category: Chappie JS]]
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[[Category: Leonard, M.]]
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[[Category: Dyda F]]
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[[Category: Schmid, S L.]]
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[[Category: Leonard M]]
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[[Category: Endocytosis]]
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[[Category: Schmid SL]]
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[[Category: Hydrolase]]
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[[Category: Membrane fission]]
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[[Category: Motor protein]]
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[[Category: Nitration]]
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[[Category: Nucleotide-binding]]
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Current revision

Dynamin 1 GTPase dimer, short axis form

PDB ID 2x2f

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