1c5k
From Proteopedia
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|PDB= 1c5k |SIZE=350|CAPTION= <scene name='initialview01'>1c5k</scene>, resolution 2.Å | |PDB= 1c5k |SIZE=350|CAPTION= <scene name='initialview01'>1c5k</scene>, resolution 2.Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=YB:YTTERBIUM (III) ION'>YB</scene> | + | |LIGAND= <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5k OCA], [http://www.ebi.ac.uk/pdbsum/1c5k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c5k RCSB]</span> | ||
}} | }} | ||
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[[Category: James, R.]] | [[Category: James, R.]] | ||
[[Category: Penfold, C N.]] | [[Category: Penfold, C N.]] | ||
| - | [[Category: YB]] | ||
[[Category: beta propellor]] | [[Category: beta propellor]] | ||
[[Category: colicin import]] | [[Category: colicin import]] | ||
[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:14:58 2008'' |
Revision as of 16:14, 30 March 2008
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| , resolution 2.Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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