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[[Image:1yxq.gif|left|200px]]


{{Structure
==Crystal structure of actin in complex with swinholide A==
|PDB= 1yxq |SIZE=350|CAPTION= <scene name='initialview01'>1yxq</scene>, resolution 2.01&Aring;
<StructureSection load='1yxq' size='340' side='right'caption='[[1yxq]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=SWI:SWINHOLIDE+A'>SWI</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
<table><tr><td colspan='2'>[[1yxq]] 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=1YXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YXQ FirstGlance]. <br>
|ACTIVITY=  
</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SWI:SWINHOLIDE+A'>SWI</scene></td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yxq OCA], [https://pdbe.org/1yxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yxq RCSB], [https://www.ebi.ac.uk/pdbsum/1yxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yxq ProSAT]</span></td></tr>
}}
</table>
== Function ==
[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;">
== Publication Abstract from PubMed ==
Marine toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds. Here we present a 2.0 A resolution structure of swinholide A, a marine macrolide, bound to two actin molecules. The structure demonstrates that the actin dimer in the complex does not represent a physiologically relevant entity, for the two actin molecules do not interact with each other. The swinholide A actin binding site is the same as that targeted by toxins of the trisoxazole family and numerous actin binding proteins, highlighting the importance of this site in actin polymerization. The observed structure reveals the mechanism of action of swinholide A and provides a structural framework about which to design new agents directed at the cytoskeleton.


'''Crystal structure of actin in complex with swinholide A'''
Structural basis of swinholide A binding to actin.,Klenchin VA, King R, Tanaka J, Marriott G, Rayment I Chem Biol. 2005 Mar;12(3):287-91. PMID:15797212<ref>PMID:15797212</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1yxq" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Marine toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds. Here we present a 2.0 A resolution structure of swinholide A, a marine macrolide, bound to two actin molecules. The structure demonstrates that the actin dimer in the complex does not represent a physiologically relevant entity, for the two actin molecules do not interact with each other. The swinholide A actin binding site is the same as that targeted by toxins of the trisoxazole family and numerous actin binding proteins, highlighting the importance of this site in actin polymerization. The observed structure reveals the mechanism of action of swinholide A and provides a structural framework about which to design new agents directed at the cytoskeleton.
*[[Actin 3D structures|Actin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1YXQ is a [[Single protein]] structure of 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=1YXQ OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structural basis of swinholide A binding to actin., Klenchin VA, King R, Tanaka J, Marriott G, Rayment I, Chem Biol. 2005 Mar;12(3):287-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15797212 15797212]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: King R]]
[[Category: King, R.]]
[[Category: Klenchin VA]]
[[Category: Klenchin, V A.]]
[[Category: Marriott G]]
[[Category: Marriott, G.]]
[[Category: Rayment I]]
[[Category: Rayment, I.]]
[[Category: Tanaka J]]
[[Category: Tanaka, J.]]
[[Category: ATP]]
[[Category: EDO]]
[[Category: MG]]
[[Category: SWI]]
[[Category: actin; swinholide a; macrolide toxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:24:44 2008''

Latest revision as of 15:25, 1 February 2023

Crystal structure of actin in complex with swinholide ACrystal structure of actin in complex with swinholide A

Structural highlights

1yxq is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 toxins targeting the actin cytoskeleton represent a new and promising class of anti-cancer compounds. Here we present a 2.0 A resolution structure of swinholide A, a marine macrolide, bound to two actin molecules. The structure demonstrates that the actin dimer in the complex does not represent a physiologically relevant entity, for the two actin molecules do not interact with each other. The swinholide A actin binding site is the same as that targeted by toxins of the trisoxazole family and numerous actin binding proteins, highlighting the importance of this site in actin polymerization. The observed structure reveals the mechanism of action of swinholide A and provides a structural framework about which to design new agents directed at the cytoskeleton.

Structural basis of swinholide A binding to actin.,Klenchin VA, King R, Tanaka J, Marriott G, Rayment I Chem Biol. 2005 Mar;12(3):287-91. PMID:15797212[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Klenchin VA, King R, Tanaka J, Marriott G, Rayment I. Structural basis of swinholide A binding to actin. Chem Biol. 2005 Mar;12(3):287-91. PMID:15797212 doi:S1074-5521(05)00067-0

1yxq, resolution 2.01Å

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