4uud

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'''Unreleased structure'''
 
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The entry 4uud is ON HOLD
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==Human dynamin 1 K44A superconstricted polymer stabilized with GTP==
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<SX load='4uud' size='340' side='right' viewer='molstar' caption='[[4uud]], [[Resolution|resolution]] 12.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4uud]] is a 12 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=4UUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UUD 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">Electron Microscopy, [[Resolution|Resolution]] 12.5&#8491;</td></tr>
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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=4uud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uud OCA], [https://pdbe.org/4uud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uud RCSB], [https://www.ebi.ac.uk/pdbsum/4uud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uud 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dynamin is a 100 kDa GTPase that organizes into helical assemblies at the base of nascent clathrin-coated vesicles. Formation of these oligomers stimulates the intrinsic GTPase activity of dynamin, which is necessary for efficient membrane fission during endocytosis. Recent evidence suggests that the transition state of dynamin's GTP hydrolysis reaction serves as a key determinant of productive fission. Here, we present the structure of a transition-state-defective dynamin mutant K44A trapped in a prefission state at 12.5 A resolution. This structure constricts to 3.7 nm, reaching the theoretical limit required for spontaneous membrane fission. Computational docking indicates that the ground-state conformation of the dynamin polymer is sufficient to achieve this superconstricted prefission state and reveals how a two-start helical symmetry promotes the most efficient packing of dynamin tetramers around the membrane neck. These data suggest a model for the assembly and regulation of the minimal dynamin fission machine.
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Authors: Sundborger, A.C., Fang, S., Heymann, J.A., Ray, P., Chappie, J.S., Hinshaw, J.E.
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A dynamin mutant defines a superconstricted prefission state.,Sundborger AC, Fang S, Heymann JA, Ray P, Chappie JS, Hinshaw JE Cell Rep. 2014 Aug 7;8(3):734-42. doi: 10.1016/j.celrep.2014.06.054. Epub 2014, Jul 31. PMID:25088425<ref>PMID:25088425</ref>
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Description: Human dynamin 1 K44A superconstricted polymer stabilized with GTP
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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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<div class="pdbe-citations 4uud" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chappie JS]]
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[[Category: Fang S]]
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[[Category: Heymann JA]]
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[[Category: Hinshaw JE]]
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[[Category: Ray P]]
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[[Category: Sundborger AC]]

Current revision

Human dynamin 1 K44A superconstricted polymer stabilized with GTP

4uud, resolution 12.50Å

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