|
|
| Line 1: |
Line 1: |
| [[Image:1tfk.gif|left|200px]] | | {{Seed}} |
| | [[Image:1tfk.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1tfk| PDB=1tfk | SCENE= }} | | {{STRUCTURE_1tfk| PDB=1tfk | SCENE= }} |
|
| |
|
| '''Ribonuclease from Escherichia coli complexed with its inhibtor protein'''
| | ===Ribonuclease from Escherichia coli complexed with its inhibtor protein=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15336558}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15336558 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_15336558}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| [[Category: Yajima, S.]] | | [[Category: Yajima, S.]] |
| [[Category: Protein-protein complex]] | | [[Category: Protein-protein complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:53:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:54:25 2008'' |