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| | <SX load='3g37' size='340' side='right' viewer='molstar' caption='[[3g37]], [[Resolution|resolution]] 6.00Å' scene=''> | | <SX load='3g37' size='340' side='right' viewer='molstar' caption='[[3g37]], [[Resolution|resolution]] 6.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g37]] is a 12 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=3G37 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3G37 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g37]] is a 12 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=3G37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G37 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3g37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g37 OCA], [http://pdbe.org/3g37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g37 RCSB], [http://www.ebi.ac.uk/pdbsum/3g37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g37 ProSAT]</span></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=3g37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g37 OCA], [https://pdbe.org/3g37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g37 RCSB], [https://www.ebi.ac.uk/pdbsum/3g37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g37 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: Murakami, K]] | + | [[Category: Murakami K]] |
| - | [[Category: Noguchi, T Q]] | + | [[Category: Noguchi TQ]] |
| - | [[Category: Uyeda, T Q]] | + | [[Category: Uyeda TQ]] |
| - | [[Category: Wakabayshi, T]] | + | [[Category: Wakabayshi T]] |
| - | [[Category: Yasunaga, T]] | + | [[Category: Yasunaga T]] |
| - | [[Category: Actin]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Cell adhesion]]
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| - | [[Category: Cellular signaling]]
| + | |
| - | [[Category: Contractile protein]]
| + | |
| - | [[Category: Cryo-em]]
| + | |
| - | [[Category: Cytokinesis]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Muscle]]
| + | |
| - | [[Category: Muscle protein]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Phosphoprotein]]
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| 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
Assembled actin filaments support cellular signaling, intracellular trafficking, and cytokinesis. ATP hydrolysis triggered by actin assembly provides the structural cues for filament turnover in vivo. Here, we present the cryo-electron microscopic (cryo-EM) structure of filamentous actin (F-actin) in the presence of phosphate, with the visualization of some alpha-helical backbones and large side chains. A complete atomic model based on the EM map identified intermolecular interactions mediated by bound magnesium and phosphate ions. Comparison of the F-actin model with G-actin monomer crystal structures reveals a critical role for bending of the conserved proline-rich loop in triggering phosphate release following ATP hydrolysis. Crystal structures of G-actin show that mutations in this loop trap the catalytic site in two intermediate states of the ATPase cycle. The combined structural information allows us to propose a detailed molecular mechanism for the biochemical events, including actin polymerization and ATPase activation, critical for actin filament dynamics.
Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release.,Murakami K, Yasunaga T, Noguchi TQ, Gomibuchi Y, Ngo KX, Uyeda TQ, Wakabayashi T Cell. 2010 Oct 15;143(2):275-87. PMID:20946985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Murakami K, Yasunaga T, Noguchi TQ, Gomibuchi Y, Ngo KX, Uyeda TQ, Wakabayashi T. Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release. Cell. 2010 Oct 15;143(2):275-87. PMID:20946985 doi:10.1016/j.cell.2010.09.034
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