1tfk: Difference between revisions
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[[Image:1tfk.gif|left|200px]] | [[Image:1tfk.gif|left|200px]] | ||
'''Ribonuclease from Escherichia coli complexed with its inhibtor protein''' | {{Structure | ||
|PDB= 1tfk |SIZE=350|CAPTION= <scene name='initialview01'>1tfk</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | |||
|ACTIVITY= | |||
|GENE= CDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), CDI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Ribonuclease from Escherichia coli complexed with its inhibtor protein''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TFK is a [ | 1TFK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFK OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15336558 15336558] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:45 2008'' | ||
Revision as of 15:17, 20 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CDA (Escherichia coli), CDI (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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