spacer
spacer

PDBsum entry 1qrs

Go to PDB code: 
Top Page protein dna_rna ligands links
Ligase/RNA PDB id
1qrs
Contents
Protein chain
529 a.a. *
DNA/RNA
Ligands
ATP
Waters ×113
* 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: 10.1021/bi961532o]
PubMed id 8942633
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 1857417
Abstract
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: 10.1126/science.2686030]
PubMed id 2686030
Full text Abstract
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: 10.1126/science.2479982]
PubMed id 2479982
Full text Abstract
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: 10.1073/pnas.81.16.5076]
PubMed id 6382258
Full text Abstract
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer