1A87

COLICIN N

Summary for 1A87

• Entry DOI: 10.2210/pdb1a87/pdb
• Descriptor: COLICIN N (2 entities in total)
• Functional Keywords: bacteriocin, toxin, pore-forming activity
• Biological source: Escherichia coli K12
• Cellular location: Cell membrane; Multi-pass membrane protein (Potential): P08083
• Total number of polymer chains: 1
• Total formula weight: 35146.27

Authors

Vetter, I.R.,Parker, M.W.,Tucker, A.D.,Lakey, J.H.,Pattus, F.,Tsernoglou, D. (deposition date: 1998-04-03, release date: 1999-04-06, Last modification date: 2024-02-07)

Primary citation

Vetter, I.R.,Parker, M.W.,Tucker, A.D.,Lakey, J.H.,Pattus, F.,Tsernoglou, D.
Crystal structure of a colicin N fragment suggests a model for toxicity.
Structure, 6:863-874, 1998

PubMed Abstract: Pore-forming colicins are water-soluble bacteriocins capable of binding to and translocating through the Escherichia coli cell envelope. They then undergo a transition to a transmembrane ion channel in the cytoplasmic membrane leading to bacterial death. Colicin N is the smallest pore-forming colicin known to date (40 kDa instead of the more usual 60 kDa) and the crystal structure of its membrane receptor, the porin OmpF, is already known. Structural knowledge of colicin N is therefore important for a molecular understanding of colicin toxicity and is relevant to toxic mechanisms in general.

PubMed: 9687368
DOI: 10.1016/S0969-2126(98)00088-4

Experimental method

X-RAY DIFFRACTION (3.1 Å)