5ooc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of jasplakinolide-stabilized F-actin in complex with ADP== | |
| + | <StructureSection load='5ooc' size='340' side='right' caption='[[5ooc]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ooc]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OOC FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9ZK:(4~{R},7~{R},10~{S},13~{S},15~{E},19~{S})-10-(4-azanylbutyl)-4-(4-hydroxyphenyl)-7-(1~{H}-indol-3-ylmethyl)-8,13,15,19-tetramethyl-1-oxa-5,8,11-triazacyclononadec-15-ene-2,6,9,12-tetrone'>9ZK</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5onv|5onv]], [[5ood|5ood]], [[5oof|5oof]], [[5ooe|5ooe]]</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=5ooc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ooc OCA], [http://pdbe.org/5ooc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ooc RCSB], [http://www.ebi.ac.uk/pdbsum/5ooc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ooc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (Pi) release results in a gradient of ATP, ADP-Pi and ADP along actin filaments (F-actin). Actin-binding proteins can recognize F-actin's nucleotide state, using it as a local 'age' tag. The underlying mechanism is complex and poorly understood. Here we report six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states. The structures reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the gamma-phosphate. Nucleotide hydrolysis and Pi release modulate the conformational ensemble at the periphery of the filament, thus resulting in open and closed states, which can be sensed by coronin-1B. The drug-like toxin jasplakinolide locks F-actin in an open state. Our results demonstrate in detail how ATP hydrolysis links to F-actin's conformational dynamics and protein interaction. | ||
| - | + | Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.,Merino F, Pospich S, Funk J, Wagner T, Kullmer F, Arndt HD, Bieling P, Raunser S Nat Struct Mol Biol. 2018 Jun;25(6):528-537. doi: 10.1038/s41594-018-0074-0. Epub, 2018 Jun 4. PMID:29867215<ref>PMID:29867215</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ooc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Arndt, H D]] | ||
| + | [[Category: Bieling, P]] | ||
| + | [[Category: Funk, J]] | ||
| + | [[Category: Kuellmer, F]] | ||
| + | [[Category: Merino, F]] | ||
| + | [[Category: Pospich, S]] | ||
| + | [[Category: Raunser, S]] | ||
| + | [[Category: Cell migration]] | ||
| + | [[Category: Cytoskeleton]] | ||
| + | [[Category: Filament stability]] | ||
| + | [[Category: Nucleotide state]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 07:30, 14 June 2018
Cryo-EM structure of jasplakinolide-stabilized F-actin in complex with ADP
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