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{{STRUCTURE_3zys| PDB=3zys | SCENE= }}
==Human dynamin 1 deltaPRD polymer stabilized with GMPPCP==
===Human dynamin 1 deltaPRD polymer stabilized with GMPPCP===
<StructureSection load='3zys' size='340' side='right' caption='[[3zys]], [[Resolution|resolution]] 12.20&Aring;' scene=''>
{{ABSTRACT_PUBMED_21962517}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3zys]] is a 6 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=3ZYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYS FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zyc|3zyc]], [[2x2f|2x2f]], [[2dyn|2dyn]], [[2x2e|2x2e]], [[1dyn|1dyn]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dynamin_GTPase Dynamin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.5 3.6.5.5] </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=3zys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zys OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zys RCSB], [http://www.ebi.ac.uk/pdbsum/3zys PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The GTPase dynamin catalyzes membrane fission by forming a collar around the necks of clathrin-coated pits, but the specific structural interactions and conformational changes that drive this process remain a mystery. We present the GMPPCP-bound structures of the truncated human dynamin 1 helical polymer at 12.2 A and a fusion protein, GG, linking human dynamin 1's catalytic G domain to its GTPase effector domain (GED) at 2.2 A. The structures reveal the position and connectivity of dynamin fragments in the assembled structure, showing that G domain dimers only form between tetramers in sequential rungs of the dynamin helix. Using chemical crosslinking, we demonstrate that dynamin tetramers are made of two dimers, in which the G domain of one molecule interacts in trans with the GED of another. Structural comparison of GG(GMPPCP) to the GG transition-state complex identifies a hydrolysis-dependent powerstroke that may play a role in membrane-remodeling events necessary for fission.


==Function==
A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke.,Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, Milligan RA, Hinshaw JE, Dyda F Cell. 2011 Sep 30;147(1):209-22. PMID:21962517<ref>PMID:21962517</ref>
[[http://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. [[http://www.uniprot.org/uniprot/MX1_HUMAN MX1_HUMAN]] Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs.<ref>PMID:20603636</ref> <ref>PMID:11880649</ref> <ref>PMID:15047845</ref> <ref>PMID:14752052</ref> <ref>PMID:15355513</ref> <ref>PMID:14687945</ref> <ref>PMID:15757897</ref> <ref>PMID:16413306</ref> <ref>PMID:16202617</ref> <ref>PMID:17374778</ref> <ref>PMID:18668195</ref> <ref>PMID:19109387</ref> <ref>PMID:21900240</ref> <ref>PMID:21992152</ref>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3zys]] is a 6 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=3ZYS OCA].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:021962517</ref><references group="xtra"/><references/>
*[[GTP-binding protein|GTP-binding protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dynamin GTPase]]
[[Category: Dynamin GTPase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chappie, J S.]]
[[Category: Chappie, J S]]
[[Category: Dyda, F.]]
[[Category: Dyda, F]]
[[Category: Fang, S.]]
[[Category: Fang, S]]
[[Category: Hinshaw, J E.]]
[[Category: Hinshaw, J E]]
[[Category: Leonard, M.]]
[[Category: Leonard, M]]
[[Category: Mears, J A.]]
[[Category: Mears, J A]]
[[Category: Milligan, R A.]]
[[Category: Milligan, R A]]
[[Category: Schmid, S L.]]
[[Category: Schmid, S L]]
[[Category: Endocytosis]]
[[Category: Endocytosis]]
[[Category: Gtp hydrolysis]]
[[Category: Gtp hydrolysis]]
[[Category: Hydrolase-gtp-binding protein complex]]
[[Category: Hydrolase-gtp-binding protein complex]]
[[Category: Membrane remodeling]]
[[Category: Membrane remodeling]]

Revision as of 10:09, 21 December 2014

Human dynamin 1 deltaPRD polymer stabilized with GMPPCP

3zys, resolution 12.20Å

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