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TitleTwo molecules of lobophorolide cooperate to stabilize an actin dimer using both their "ring" and "tail" region.
Journal, issue, pagesChem. Biol., Vol. 17, Page 802-807, Year 2010
Publish dateMar 15, 2010 (structure data deposition date)
AuthorsBlain, J.C. / Mok, Y.F. / Kubanek, J. / Allingham, J.S.
External linksChem. Biol. / PubMed:20797609
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-3m6g:
Crystal structure of actin in complex with lobophorolide
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-LO3:
(1S,3S,4S,5S,7R,8S,9R,12E,14E,16R,17R,19R)-16-hydroxy-9-{(1S,2S,3S)-2-hydroxy-5-[(2S,4R,6S)-4-methoxy-6-methyltetrahydro-2H-pyran-2-yl]-1,3-dimethylpentyl}-3,5,7,17-tetramethoxy-8,14-dimethyl-11H-spiro[10,23-dioxabicyclo[17.3.1]tricosa-12,14,20-triene-4,2'-oxiran]-11-one

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • oryctolagus cuniculus (rabbit)
KeywordsSTRUCTURAL PROTEIN / Actin / macrolide / lobophorolide / actin dimer / marine toxin / ATP-binding / Cytoskeleton / Muscle protein / Nucleotide-binding

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