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PDBsum entry 1m1c
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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L-A virus at 3.4 a resolution reveals particle architecture and mRNA decapping mechanism.
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Authors
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H.Naitow,
J.Tang,
M.Canady,
R.B.Wickner,
J.E.Johnson.
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Ref.
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Nat Struct Biol, 2002,
9,
725-728.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the yeast L-A virus was determined by X-ray crystallography at
3.4 A resolution. The L-A dsRNA virus is 400 A in diameter and contains a single
protein shell of 60 asymmetric dimers of the coat protein, a feature common
among the inner protein shells of dsRNA viruses and probably related to their
unique mode of transcription and replication. The two identical subunits in each
dimer are in non-equivalent environments and show substantially different
conformations in specific surface regions. The L-A virus decaps cellular mRNA to
efficiently translate its own uncapped mRNA. Our structure reveals a trench at
the active site of the decapping reaction and suggests a role for nearby
residues in the reaction.
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Figure 2.
Figure 2. A region of the electron density map is shown fit with
residues 106 -114 (Ser-His-Ala-Tyr-Asn-Ile-Thr-Ser-Trp).
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Figure 4.
Figure 4. A stereo view close-up of the trench showing residue
His 154 and its neighboring residues around the active site.
Residues Tyr 150, His 151, Asp 152, Tyr 452, Tyr 538 and Asp 540
all may contribute to the mRNA decapping reaction. The four
loops corresponding to loop 1, 2, 3 and 4, are colored in red,
green, blue and pink, respectively.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2002,
9,
725-728)
copyright 2002.
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Secondary reference #1
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Title
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La virus: a virus capsid with enzymatic mRNA decapping activity
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Authors
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J.Tang,
H.Naitow,
L.Tang,
R.B.Wickner,
J.E.Johnson.
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Ref.
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TO BE PUBLISHED ...
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