|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1rfq' size='340' side='right'caption='[[1rfq]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1rfq' size='340' side='right'caption='[[1rfq]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rfq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RFQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rfq]] is a 2 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=1RFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RFQ 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=LAR:LATRUNCULIN+A'>LAR</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">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rdw|1rdw]]</div></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=LAR:LATRUNCULIN+A'>LAR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTA1, ACTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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=1rfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfq OCA], [https://pdbe.org/1rfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rfq RCSB], [https://www.ebi.ac.uk/pdbsum/1rfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rfq 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=1rfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfq OCA], [http://pdbe.org/1rfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rfq RCSB], [http://www.ebi.ac.uk/pdbsum/1rfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rfq 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 == |
| Line 27: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: European rabbit]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Agbandje-McKenna, M]] | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Bubb, M R]] | + | [[Category: Agbandje-McKenna M]] |
| - | [[Category: Govindasamy, L]] | + | [[Category: Bubb MR]] |
| - | [[Category: McKenna, R]] | + | [[Category: Govindasamy L]] |
| - | [[Category: Reutzel, R]] | + | [[Category: McKenna R]] |
| - | [[Category: Yarmola, E G]] | + | [[Category: Reutzel R]] |
| - | [[Category: Yoshioka, C]] | + | [[Category: Yarmola EG]] |
| - | [[Category: Anti-parallel dimer]]
| + | [[Category: Yoshioka C]] |
| - | [[Category: Filament]]
| + | |
| - | [[Category: Nucleation]]
| + | |
| - | [[Category: Polymerization]]
| + | |
| - | [[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
Actin filament nucleation, polymerization, and branching are crucial steps in many forms of cell motility, cell shape, and intracellular organelle movements in a wide range of organisms. Previous biochemical data suggests that an anti-parallel actin dimer can incorporate itself into growing filamentous actin (F-actin) and has a role in branching. Furthermore, it is a widespread belief that nucleation is spawned from an actin trimer complex. Here we present the structures of actin dimers and trimers in two tetragonal crystal systems P4(3)2(1)2 and P4(3). Both crystal systems formed by an induced condensation transformation of a previously reported orthorhombic crystal system P2(1)2(1)2(1). Comparison between the three crystal systems demonstrates the dynamics and flexibility of actin-actin interactions. The dimer and trimer actin rearrangements observed between the three crystal systems may provide insight to in vivo actin-actin interactions that occur during the nucleation, polymerization, and branching of F-actin.
Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer.,Reutzel R, Yoshioka C, Govindasamy L, Yarmola EG, Agbandje-McKenna M, Bubb MR, McKenna R J Struct Biol. 2004 Jun;146(3):291-301. PMID:15099571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reutzel R, Yoshioka C, Govindasamy L, Yarmola EG, Agbandje-McKenna M, Bubb MR, McKenna R. Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer. J Struct Biol. 2004 Jun;146(3):291-301. PMID:15099571 doi:10.1016/j.jsb.2003.12.006
|
