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PDBsum entry 3tuy
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Structural protein
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PDB id
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3tuy
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Contents |
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69 a.a.
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141 a.a.
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152 a.a.
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PDB id:
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Structural protein
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Title:
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Phosphorylated light chain domain of scallop smooth muscle myosin
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Structure:
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Myosin heavy chain. Chain: a, d. Myosin regulatory light chain. Chain: b, e. Myosin essential light chain. Chain: c, f
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Source:
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Placopecten magellanicus. Sea scallop. Organism_taxid: 6577. Organism_taxid: 6577
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Resolution:
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2.50Å
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R-factor:
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0.201
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R-free:
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0.252
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Authors:
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V.S.S.Kumar,E.O'Neall-Hennessey,L.Reshetnikova,J.H.Brown,H.Robinson, A.G.Szent-Gyorgyi,C.Cohen
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Key ref:
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V.S.Kumar
et al.
(2011).
Crystal structure of a phosphorylated light chain domain of scallop smooth-muscle myosin.
Biophys J,
101,
2185-2189.
PubMed id:
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Date:
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19-Sep-11
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Release date:
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23-Nov-11
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PROCHECK
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Headers
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References
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Q26080
(Q26080_PLAMG) -
Myosin heavy chain from Placopecten magellanicus
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Seq:
Struc:
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1950 a.a.
69 a.a.
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Biophys J
101:2185-2189
(2011)
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PubMed id:
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Crystal structure of a phosphorylated light chain domain of scallop smooth-muscle myosin.
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V.S.Kumar,
E.O'Neall-Hennessey,
L.Reshetnikova,
J.H.Brown,
H.Robinson,
A.G.Szent-Györgyi,
C.Cohen.
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ABSTRACT
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We have determined the crystal structure of a phosphorylated smooth-muscle
myosin light chain domain (LCD). This reconstituted LCD is of a sea scallop
catch muscle myosin with its phosphorylatable regulatory light chain (RLC SmoA).
In the crystal structure, Arg(16), an arginine residue that is present in this
isoform but not in vertebrate smooth-muscle RLC, stabilizes the phosphorylation
site. This arginine interacts with the carbonyl group of the
phosphorylation-site serine in the unphosphorylated LCD (determined previously),
and with the phosphate group when the serine is phosphorylated. However, the
overall conformation of the LCD is essentially unchanged upon phosphorylation.
This result provides additional evidence that phosphorylation of the RLC is
unlikely to act as an on-switch in regulation of scallop catch muscle myosin.
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Links
