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| <StructureSection load='3b5u' size='340' side='right'caption='[[3b5u]], [[Resolution|resolution]] 9.50Å' scene=''> | | <StructureSection load='3b5u' size='340' side='right'caption='[[3b5u]], [[Resolution|resolution]] 9.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3b5u]] is a 14 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=3B5U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3B5U FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3b5u]] is a 14 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=3B5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B5U FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1atn|1atn]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 9.5Å</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=3b5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5u OCA], [http://pdbe.org/3b5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3b5u RCSB], [http://www.ebi.ac.uk/pdbsum/3b5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3b5u 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=3b5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5u OCA], [https://pdbe.org/3b5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b5u RCSB], [https://www.ebi.ac.uk/pdbsum/3b5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b5u 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;">
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| == Publication Abstract from PubMed ==
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| Actin carries out many of its cellular functions through its filamentous form; thus, understanding the detailed structure of actin filaments is an essential step in achieving a mechanistic understanding of actin function. The acrosomal bundle in the Limulus sperm has been shown to be a quasi-crystalline array with an asymmetric unit composed of a filament with 14 actin-scruin pairs. The bundle in its true discharge state penetrates the jelly coat of the egg. Our previous electron crystallographic reconstruction demonstrated that the actin filament cross-linked by scruin in this acrosomal bundle state deviates significantly from a perfect F-actin helix. In that study, the tertiary structure of each of the 14 actin protomers in the asymmetric unit of the bundle filament was assumed to be constant. In the current study, an actin filament atomic model in the acrosomal bundle has been refined by combining rigid-body docking with multiple actin crystal structures from the Protein Data Bank and constrained energy minimization. Our observation demonstrates that actin protomers adopt different tertiary conformations when they form an actin filament in the bundle. The scruin and bundle packing forces appear to influence the tertiary and quaternary conformations of actin in the filament of this biologically active bundle.
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| Crystallographic conformers of actin in a biologically active bundle of filaments.,Cong Y, Topf M, Sali A, Matsudaira P, Dougherty M, Chiu W, Schmid MF J Mol Biol. 2008 Jan 11;375(2):331-6. Epub 2007 Oct 16. PMID:18022194<ref>PMID:18022194</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3b5u" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Actin 3D structures|Actin 3D structures]] | | *[[Actin 3D structures|Actin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| [[Category: Chiu, W]] | | [[Category: Chiu W]] |
| [[Category: Cong, Y]] | | [[Category: Cong Y]] |
| [[Category: Dougherty, M]] | | [[Category: Dougherty M]] |
| [[Category: Matsudaira, P]] | | [[Category: Matsudaira P]] |
| [[Category: Sali, A]] | | [[Category: Sali A]] |
| [[Category: Schmid, M F]] | | [[Category: Schmid MF]] |
| [[Category: Topf, M]] | | [[Category: Topf M]] |
| [[Category: Acromsomal bundle]]
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| [[Category: Actin]]
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| [[Category: Actin filament]]
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| [[Category: Cryoem]]
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| [[Category: Motor protein]]
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