1c5k
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(New page: 200px<br /><applet load="1c5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c5k, resolution 2.Å" /> '''THE STRUCTURE OF TOLB,...)
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Revision as of 10:03, 20 November 2007
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THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9
Overview
BACKGROUND: E colicin proteins have three functional domains, each of, which is implicated in one of the stages of killing Escherichia coli, cells: receptor binding, translocation and cytotoxicity. The central (R), domain is responsible for receptor-binding activity whereas the N-terminal, (T) domain mediates translocation, the process by which the C-terminal, cytotoxic domain is transported from the receptor to the site of its, cytotoxicity. The translocation of enzymatic E colicins like colicin E9 is, dependent upon TolB but the details of the process are not known. RESULTS:, We have demonstrated a protein-protein interaction between the T domain of, colicin E9 and TolB, an essential component of the tol-dependent, translocation system in E. coli, using the yeast two-hybrid system. The, crystal structure of TolB, a procaryotic tryptophan-aspartate (WD) repeat, protein, reveals an N-terminal alpha + beta domain based on a, five-stranded mixed beta sheet and a C-terminal six-bladed beta-propeller, domain. CONCLUSIONS: The results suggest that the TolB-box residues of the, T domain of colicin E9 interact with the beta-propeller domain of TolB., The protein-protein interactions of other beta-propeller-containing, proteins, the yeast yPrp4 protein and G proteins, are mediated by the, loops or outer sheets of the propeller blades. The determination of the, three-dimensional structure of the T domain-TolB complex and the isolation, of mutations in TolB that abolish the interaction with the T domain will, reveal fine details of the protein-protein interaction of TolB and the T, domain of E colicins.
About this Structure
1C5K is a Single protein structure of sequence from Escherichia coli with YB as ligand. Full crystallographic information is available from OCA.
Reference
The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9., Carr S, Penfold CN, Bamford V, James R, Hemmings AM, Structure. 2000 Jan 15;8(1):57-66. PMID:10673426
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