1tfk
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Ribonuclease from Escherichia coli complexed with its inhibtor protein
OverviewOverview
Colicin D is a plasmid-encoded proteinaceous toxin which kills sensitive, Escherichia coli. Toxicity stems from ribonuclease activity that targets, exclusively four isoacceptors of tRNA(Arg) with a cleavage position, between 38 and 39 of the corresponding anticodons. Since no other tRNAs, with the same sequences at 38 and 39 as tRNA(Arg)s are cleaved, colicin D, should be capable of recognizing some higher order structure of tRNAs. We, report here two crystal structures of catalytic domains of colicin D which, have different N-terminal lengths, both complexed with its cognate, inhibitor protein, ImmD. A row of positive charge patches is found on the, surface of the catalytic domain, suggestive of the binding site of the, tRNAs. This finding, together with our refined tRNase activity, experiments, indicates that the catalytic domain starting at position 595, has activity almost equivalent to that of colicin D.
About this StructureAbout this Structure
1TFK is a Protein complex structure of sequences from Escherichia coli with MES as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Relation between tRNase activity and the structure of colicin D according to X-ray crystallography., Yajima S, Nakanishi K, Takahashi K, Ogawa T, Hidaka M, Kezuka Y, Nonaka T, Ohsawa K, Masaki H, Biochem Biophys Res Commun. 2004 Sep 24;322(3):966-73. PMID:15336558
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