1O82

X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM

Summary for 1O82

• Entry DOI: 10.2210/pdb1o82/pdb
• Related: 1E68 1O83 1O84
• Descriptor: PEPTIDE ANTIBIOTIC AS-48, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: peptide antibiotic, bacteriocin, cationic antibacterial peptides, membrane permeabilization, protein crystallography, cyclic polypeptide, protein membrane interaction
• Biological source: ENTEROCOCCUS FAECALIS (STREPTOCOCCUS LIQUEFACIENS)
• Total number of polymer chains: 4
• Total formula weight: 29282.56

Authors

Sanchez-Barrena, M.J.,Martinez-Ripoll, M.,Galvez, A.,Martinez-Bueno, M.,Maqueda, M.,Cruz, V.,Albert, A. (deposition date: 2002-11-22, release date: 2003-11-20, Last modification date: 2024-05-08)

Primary citation

Sanchez-Barrena, M.J.,Martinez-Ripoll, M.,Galvez, A.,Valdivia, E.,Maqueda, M.,Cruz, V.,Albert, A.
Structure of Bacteriocin as-48: From Soluble State to Membrane Bound State
J.Mol.Biol., 334:541-, 2003

PubMed Abstract: The bacteriocin AS-48 is a membrane-interacting peptide, which displays a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. The NMR structure of AS-48 at pH 3 has been solved. The analysis of this structure suggests that the mechanism of AS-48 anti-bacterial activity involves the accumulation of positively charged molecules at the membrane surface leading to a disruption of the membrane potential. Here, we report the high-resolution crystal structure of AS-48 and sedimentation equilibrium experiments showing that this bacteriocin is able to adopt different oligomeric structures according to the physicochemical environment. The analysis of these structures suggests a mechanism for molecular function of AS-48 involving a transition from a water-soluble form to a membrane-bound state upon membrane binding.

PubMed: 14623193
DOI: 10.1016/J.JMB.2003.09.060

Experimental method

X-RAY DIFFRACTION (1.46 Å)