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| | <StructureSection load='1qz5' size='340' side='right'caption='[[1qz5]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='1qz5' size='340' side='right'caption='[[1qz5]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qz5]] is a 1 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=1QZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QZ5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qz5]] is a 1 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=1QZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZ5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=KAB:KABIRAMIDE+C'>KAB</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]] 1.45Å</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=KAB:KABIRAMIDE+C'>KAB</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qz6|1qz6]]</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=1qz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qz5 OCA], [https://pdbe.org/1qz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1qz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qz5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qz5 OCA], [http://pdbe.org/1qz5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qz5 RCSB], [http://www.ebi.ac.uk/pdbsum/1qz5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qz5 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: Allingham, J S]] | + | [[Category: Allingham JS]] |
| - | [[Category: King, R]] | + | [[Category: King R]] |
| - | [[Category: Klenchin, V A]] | + | [[Category: Klenchin VA]] |
| - | [[Category: Marriott, G]] | + | [[Category: Marriott G]] |
| - | [[Category: Rayment, I]] | + | [[Category: Rayment I]] |
| - | [[Category: Tanaka, J]] | + | [[Category: Tanaka J]] |
| - | [[Category: Actin]]
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| - | [[Category: Kabiramide c]]
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| - | [[Category: Structural protein]]
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| - | [[Category: Toxin]]
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| - | [[Category: Trisoxazole]]
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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
Marine macrolide toxins of trisoxazole family target actin with high affinity and specificity and have promising pharmacological properties. We present X-ray structures of actin in complex with two members of this family, kabiramide C and jaspisamide A, at a resolution of 1.45 and 1.6 A, respectively. The structures reveal the absolute stereochemistry of these toxins and demonstrate that their trisoxazole ring interacts with actin subdomain 1 while the aliphatic side chain is inserted into the hydrophobic cavity between actin subdomains 1 and 3. The binding site is essentially the same as the one occupied by the actin-capping domain of the gelsolin superfamily of proteins. The structural evidence suggests that actin filament severing and capping by these toxins is also analogous to that of gelsolin. Consequently, these macrolides may be viewed as small molecule biomimetics of an entire class of actin-binding proteins.
Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin.,Klenchin VA, Allingham JS, King R, Tanaka J, Marriott G, Rayment I Nat Struct Biol. 2003 Dec;10(12):1058-63. Epub 2003 Oct 26. PMID:14578936[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Klenchin VA, Allingham JS, King R, Tanaka J, Marriott G, Rayment I. Trisoxazole macrolide toxins mimic the binding of actin-capping proteins to actin. Nat Struct Biol. 2003 Dec;10(12):1058-63. Epub 2003 Oct 26. PMID:14578936 doi:10.1038/nsb1006
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