 |
PDBsum entry 1qrs
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Crystal structures of three misacylating mutants of escherichia coli glutaminyl-Trna synthetase complexed with tRNA(gln) and ATP.
|
 |
|
Authors
|
 |
J.G.Arnez,
T.A.Steitz.
|
 |
|
Ref.
|
 |
Biochemistry, 1996,
35,
14725-14733.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
|
 |
 |
|
Abstract
|
 |
|
Three previously described mutant Escherichia coli glutaminyl-tRNA synthetase
(GlnRS) proteins that incorrectly aminoacylate the amber suppressor derived from
tRNATyr (supF) with glutamine were cocrystallized with wild-type tRNAGln and
their structures determined. In two of the mutant enzymes studied, Asp235, which
contacts base pair G3-C70 in the acceptor stem, has been changed to asparagine
in GlnRS7 and to glycine in GlnRS10. These mutations result in changed
interactions between Asn235 of GlnRS7 and G3-C70 of the tRNA and an altered
water structure between Gly235 of GlnRS10 and base pair G3-C70. These structures
suggest how the mutant enzymes can show only small changes in their ability to
aminoacylate wild-type cognate tRNA on the one hand and yet show a lack of
discrimination against a noncognate U3-A70 base pair on the other. In contrast,
the change of Ile129 to Thr in GlnRS15 causes virtually no change in the
structure of the complex, and the explanation for its ability to misacylate supF
is unclear.
|
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
Structural basis of anticodon loop recognition by glutaminyl-Trna synthetase.
|
 |
|
Authors
|
 |
M.A.Rould,
J.J.Perona,
T.A.Steitz.
|
 |
|
Ref.
|
 |
Nature, 1991,
352,
213-218.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #2
|
 |
|
Title
|
 |
Structural basis for misaminoacylation by mutant e. Coli glutaminyl-Trna synthetase enzymes.
|
 |
|
Authors
|
 |
J.J.Perona,
R.N.Swanson,
M.A.Rould,
T.A.Steitz,
D.Söll.
|
 |
|
Ref.
|
 |
Science, 1989,
246,
1152-1154.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #3
|
 |
|
Title
|
 |
Structure of e. Coli glutaminyl-Trna synthetase complexed with tRNA(gln) and ATP at 2.8 a resolution.
|
 |
|
Authors
|
 |
M.A.Rould,
J.J.Perona,
D.Söll,
T.A.Steitz.
|
 |
|
Ref.
|
 |
Science, 1989,
246,
1135-1142.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #4
|
 |
|
Title
|
 |
Transfer RNA mischarging mediated by a mutant escherichia coli glutaminyl-Trna synthetase.
|
 |
|
Authors
|
 |
H.Inokuchi,
P.Hoben,
F.Yamao,
H.Ozeki,
D.Söll.
|
 |
|
Ref.
|
 |
Proc Natl Acad Sci U S A, 1984,
81,
5076-5080.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
|
|
|
 |