1tfk: Difference between revisions

Revision as of 06:54, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tfk.png

Template:STRUCTURE 1tfk

Ribonuclease from Escherichia coli complexed with its inhibtor proteinRibonuclease from Escherichia coli complexed with its inhibtor protein

Template:ABSTRACT PUBMED 15336558

About this StructureAbout this Structure

1TFK is a Protein complex structure of sequences from Escherichia coli. 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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OCA

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-'''Ribonuclease from Escherichia coli complexed with its inhibtor protein'''
+===Ribonuclease from Escherichia coli complexed with its inhibtor protein===
-==Overview==
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-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.
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 [[Category: Yajima, S.]]
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