3zys

From Proteopedia

(Difference between revisions)

Current revision

Human dynamin 1 deltaPRD polymer stabilized with GMPPCP

3zys, resolution 12.20Å

Structural highlights

3zys is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 12.2Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chappie JS, Mears JA, Fang S, Leonard M, Schmid SL, Milligan RA, Hinshaw JE, Dyda F. A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke. Cell. 2011 Sep 30;147(1):209-22. PMID:21962517 doi:10.1016/j.cell.2011.09.003

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zys"

@@ Line 1: / Line 1: @@
-{{STRUCTURE_3zys|  PDB=3zys  |  SCENE=  }}
-===Human dynamin 1 deltaPRD polymer stabilized with GMPPCP===
-{{ABSTRACT_PUBMED_21962517}}
-==Function==
+==Human dynamin 1 deltaPRD polymer stabilized with GMPPCP==
-[[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>
+<SX load='3zys' size='340' side='right' viewer='molstar' caption='[[3zys]], [[Resolution|resolution]] 12.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3zys]] is a 6 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=3ZYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYS FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 12.2&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zys OCA], [https://pdbe.org/3zys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zys RCSB], [https://www.ebi.ac.uk/pdbsum/3zys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zys ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+<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.
-==About this Structure==
+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>
-[[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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:021962517</ref><references group="xtra"/><references/>
+</div>
-[[Category: Dynamin GTPase]]
+<div class="pdbe-citations 3zys" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
 [[Category: Homo sapiens]]
-[[Category: Chappie, J S.]]
+[[Category: Large Structures]]
-[[Category: Dyda, F.]]
+[[Category: Chappie JS]]
-[[Category: Fang, S.]]
+[[Category: Dyda F]]
-[[Category: Hinshaw, J E.]]
+[[Category: Fang S]]
-[[Category: Leonard, M.]]
+[[Category: Hinshaw JE]]
-[[Category: Mears, J A.]]
+[[Category: Leonard M]]
-[[Category: Milligan, R A.]]
+[[Category: Mears JA]]
-[[Category: Schmid, S L.]]
+[[Category: Milligan RA]]
-[[Category: Endocytosis]]
+[[Category: Schmid SL]]
-[[Category: Gtp hydrolysis]]
-[[Category: Hydrolase-gtp-binding protein complex]]
-[[Category: Membrane remodeling]]

3zys

From Proteopedia

Current revision

Human dynamin 1 deltaPRD polymer stabilized with GMPPCP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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