1C5K

THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9

Summary for 1C5K

• Entry DOI: 10.2210/pdb1c5k/pdb
• Descriptor: PROTEIN (TOLB PROTEIN), YTTERBIUM (III) ION (3 entities in total)
• Functional Keywords: beta propellor, protein-protein interactions, colicin import, transport protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 47369.63

Authors

Carr, S.,Penfold, C.N.,Bamford, V.,James, R.,Hemmings, A.M. (deposition date: 1999-12-05, release date: 2000-12-06, Last modification date: 2023-12-27)

Primary citation

Carr, S.,Penfold, C.N.,Bamford, V.,James, R.,Hemmings, A.M.
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.
Structure Fold.Des., 8:57-66, 2000

PubMed Abstract: 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.

PubMed: 10673426
DOI: 10.1016/S0969-2126(00)00079-4

Experimental method

X-RAY DIFFRACTION (2 Å)