1v74
From Proteopedia
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| - | [[Image:1v74.gif|left|200px]] | + | [[Image:1v74.gif|left|200px]] |
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| - | '''ribonuclease-inhibitor complex''' | + | {{Structure |
| + | |PDB= 1v74 |SIZE=350|CAPTION= <scene name='initialview01'>1v74</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE GLYCOL'>1PE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''ribonuclease-inhibitor complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V74 is a [ | + | 1V74 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=1V74 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein., Graille M, Mora L, Buckingham RH, van Tilbeurgh H, de Zamaroczy M, EMBO J. 2004 Apr 7;23(7):1474-82. Epub 2004 Mar 11. PMID:[http:// | + | Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein., Graille M, Mora L, Buckingham RH, van Tilbeurgh H, de Zamaroczy M, EMBO J. 2004 Apr 7;23(7):1474-82. Epub 2004 Mar 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15014439 15014439] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transfer rnase]] | [[Category: transfer rnase]] | ||
| - | ''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 14:41:43 2008'' |
Revision as of 12:41, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ribonuclease-inhibitor complex
Overview
Colicins are toxins secreted by Escherichia coli in order to kill their competitors. Colicin D is a 75 kDa protein that consists of a translocation domain, a receptor-binding domain and a cytotoxic domain, which specifically cleaves the anticodon loop of all four tRNA(Arg) isoacceptors, thereby inactivating protein synthesis and leading to cell death. Here we report the 2.0 A resolution crystal structure of the complex between the toxic domain and its immunity protein ImmD. Neither component shows structural homology to known RNases or their inhibitors. In contrast to other characterized colicin nuclease-Imm complexes, the colicin D active site pocket is completely blocked by ImmD, which, by bringing a negatively charged cluster in opposition to a positively charged cluster on the surface of colicin D, appears to mimic the tRNA substrate backbone. Site-directed mutations affecting either the catalytic domain or the ImmD protein have led to the identification of the residues vital for catalytic activity and for the tight colicin D/ImmD interaction that inhibits colicin D toxicity and tRNase catalytic activity.
About this Structure
1V74 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein., Graille M, Mora L, Buckingham RH, van Tilbeurgh H, de Zamaroczy M, EMBO J. 2004 Apr 7;23(7):1474-82. Epub 2004 Mar 11. PMID:15014439
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