This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1c5k
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[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
| |||||||
| , resolution 2.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| 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
Page seeded by OCA on Sun Mar 30 19:14:58 2008
