1ffy
|
INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN
OverviewOverview
Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at, its synthetic active site and hydrolyzes incorrectly acylated amino acids, at its editing active site. The 2.2 angstrom resolution crystal structure, of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin, shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active, site. To position the 3' terminus in the synthetic active site, the, acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln), complexed with its synthetase. The amino acid editing activity of the, IleRS may result from the incorrect products shuttling between the, synthetic and editing active sites, which is reminiscent of the editing, mechanism of DNA polymerases.
About this StructureAbout this Structure
1FFY is a Single protein structure of sequence from Staphylococcus aureus with K, ZN, MG and MRC as ligands. The following page contains interesting information on the relation of 1FFY with [Aminoacyl-tRNA Synthetases]. Active as Isoleucine--tRNA ligase, with EC number 6.1.1.5 Full crystallographic information is available from OCA.
ReferenceReference
Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin., Silvian LF, Wang J, Steitz TA, Science. 1999 Aug 13;285(5430):1074-7. PMID:10446055
Page seeded by OCA on Sun Nov 18 09:00:09 2007