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PDBsum entry 2ct8
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References listed in PDB file
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Key reference
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Title
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Structural basis for anticodon recognition by methionyl-Trna synthetase.
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Authors
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K.Nakanishi,
Y.Ogiso,
T.Nakama,
S.Fukai,
O.Nureki.
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Ref.
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Nat Struct Biol, 2005,
12,
931-932.
[DOI no: ]
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PubMed id
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Abstract
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In the 2.7-A resolution crystal structure of methionyl-tRNA synthetase (MetRS)
in complex with tRNA(Met) and a methionyl-adenylate analog, the tRNA anticodon
loop is distorted to form a triple-base stack comprising C34, A35 and A38. A
tryptophan residue stacks on C34 to extend the triple-base stack. In addition,
C34 forms Watson-Crick-type hydrogen bonds with Arg357. This structure resolves
the longstanding question of how MetRS specifically recognizes tRNA(Met).
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Figure 1.
Figure 1. The A. aeolicus MetRS−tRNA[m]^Met complex. Green,
the Rossmann fold domain; cyan and dark blue, the CP1 and CP2
insertions, respectively; salmon, the MetRS-specific  -strand
insertion; red, the stem-contact-fold domain; pink, the  -helix
bundle domain; yellow, tRNA[m]^Met; stick model, MetSA.
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Figure 2.
Figure 2. Recognition of the anticodon CAU of tRNA[m]^Met by
MetRS. (a) Conformational change of A. aeolicus tRNA[m]^Met
(yellow) upon binding MetRS, as compared with unbound yeast
tRNA^Phe (blue). (b) Interaction between MetRS and the
tRNA[m]^Met anticodon. Yellow, tRNA[m]^Met nucleotides; light
purple, MetRS residues; dotted lines, hydrogen bonds; red,
oxygen; blue, nitrogen.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2005,
12,
931-932)
copyright 2005.
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