3zyc

From Proteopedia

(Difference between revisions)

Current revision

DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP

Structural highlights

3zyc is a 2 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:	X-ray diffraction, Resolution 2.2Å
Ligands:	,
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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-[[Image:3zyc.png|left|200px]]
-<!--
+==DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP==
-The line below this paragraph, containing "STRUCTURE_3zyc", creates the "Structure Box" on the page.
+<StructureSection load='3zyc' size='340' side='right'caption='[[3zyc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3zyc]] 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=3ZYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYC FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_3zyc|  PDB=3zyc  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyc OCA], [https://pdbe.org/3zyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyc RCSB], [https://www.ebi.ac.uk/pdbsum/3zyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyc 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.
-===DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_21962517}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3zyc" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21962517 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21962517}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[3zyc]] 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=3ZYC OCA].
-==Reference==
-<ref group="xtra">PMID:021962517</ref><references group="xtra"/>
 [[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: Hydrolase]]
-[[Category: Membrane fission]]
-[[Category: Motor protein]]
-[[Category: Nucleotide-binding]]

3zyc

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Current revision

DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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