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| | <SX load='5ooe' size='340' side='right' viewer='molstar' caption='[[5ooe]], [[Resolution|resolution]] 3.60Å' scene=''> | | <SX load='5ooe' size='340' side='right' viewer='molstar' caption='[[5ooe]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ooe]] 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=5OOE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OOE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ooe]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OOE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5onv|5onv]], [[5ooc|5ooc]], [[5ood|5ood]], [[5oof|5oof]]</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=5ooe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ooe OCA], [https://pdbe.org/5ooe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ooe RCSB], [https://www.ebi.ac.uk/pdbsum/5ooe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ooe ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ooe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ooe OCA], [http://pdbe.org/5ooe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ooe RCSB], [http://www.ebi.ac.uk/pdbsum/5ooe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ooe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Arndt, H D]] | + | [[Category: Arndt H-D]] |
| - | [[Category: Bieling, P]] | + | [[Category: Bieling P]] |
| - | [[Category: Funk, J]] | + | [[Category: Funk J]] |
| - | [[Category: Kuellmer, F]] | + | [[Category: Kuellmer F]] |
| - | [[Category: Merino, F]] | + | [[Category: Merino F]] |
| - | [[Category: Pospich, S]] | + | [[Category: Pospich S]] |
| - | [[Category: Raunser, S]] | + | [[Category: Raunser S]] |
| - | [[Category: Cell migration]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Filament stability]]
| + | |
| - | [[Category: Nucleotide state]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Merino F, Pospich S, Funk J, Wagner T, Kullmer F, Arndt HD, Bieling P, Raunser S. Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM. Nat Struct Mol Biol. 2018 Jun;25(6):528-537. doi: 10.1038/s41594-018-0074-0. Epub, 2018 Jun 4. PMID:29867215 doi:http://dx.doi.org/10.1038/s41594-018-0074-0
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