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| <StructureSection load='5ypu' size='340' side='right'caption='[[5ypu]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5ypu' size='340' side='right'caption='[[5ypu]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5ypu]] is a 4 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=5YPU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YPU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ypu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YPU FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</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=5ypu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ypu OCA], [http://pdbe.org/5ypu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ypu RCSB], [http://www.ebi.ac.uk/pdbsum/5ypu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ypu 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=5ypu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ypu OCA], [https://pdbe.org/5ypu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ypu RCSB], [https://www.ebi.ac.uk/pdbsum/5ypu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ypu 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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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| + | [[Category: Mus musculus]] |
| [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
- | [[Category: Ferrer, F J]] | + | [[Category: Ferrer FJ]] |
- | [[Category: Robinson, R C]] | + | [[Category: Robinson RC]] |
- | [[Category: Scipion, C P.M]] | + | [[Category: Scipion CPM]] |
- | [[Category: Wongsantichon, J]] | + | [[Category: Wongsantichon J]] |
- | [[Category: Yuen, T Y]] | + | [[Category: Yuen TY]] |
- | [[Category: Actin-binding]]
| + | |
- | [[Category: Nucleation]]
| + | |
- | [[Category: Peptide binding protein]]
| + | |
- | [[Category: Wh2]]
| + | |
| 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 structure of the actin filament is known at a resolution that has allowed the architecture of protein components to be unambiguously assigned. However, fully understanding the chemistry of the system requires higher resolution to identify the ions and water molecules involved in polymerization and ATP hydrolysis. Here, we find experimental evidence for the association of cations with the surfaces of G-actin in a 2.0-A resolution X-ray structure of actin bound to a Cordon-Bleu WH2 motif and in previously determined high-resolution X-ray structures. Three of four reoccurring divalent cation sites were stable during molecular dynamics (MD) simulations of the filament, suggesting that these sites may play a functional role in stabilizing the filament. We modeled the water coordination at the ATP-bound Mg(2+), which also proved to be stable during the MD simulations. Using this model of the filament with a hydrated ATP-bound Mg(2+), we compared the cumulative probability of an activated hydrolytic water molecule approaching the gamma-phosphorous of ATP, in comparison with G-actin, in the MD simulations. The cumulative probability increased in F-actin in line with the activation of actin's ATPase activity on polymerization. However, inclusion of the cations in the filament lowered cumulative probability, suggesting the rate of hydrolysis may be linked to filament flexibility. Together, these data extend the possible roles of Mg(2+) in polymerization and the mechanism of polymerization-induced activation of actin's ATPase activity.
Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.,Scipion CPM, Ghoshdastider U, Ferrer FJ, Yuen TY, Wongsantichon J, Robinson RC Proc Natl Acad Sci U S A. 2018 Sep 25. pii: 1806394115. doi:, 10.1073/pnas.1806394115. PMID:30254171[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Scipion CPM, Ghoshdastider U, Ferrer FJ, Yuen TY, Wongsantichon J, Robinson RC. Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis. Proc Natl Acad Sci U S A. 2018 Sep 25. pii: 1806394115. doi:, 10.1073/pnas.1806394115. PMID:30254171 doi:http://dx.doi.org/10.1073/pnas.1806394115
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