1o82 | pdb_00001o82
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X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM
Overview
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 ... [(full description)]
About this Structure
1O82 is a [Single protein] structure of sequence from [Enterococcus faecalis] with SO4 and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of bacteriocin AS-48: from soluble state to membrane bound state., Sanchez-Barrena MJ, Martinez-Ripoll M, Galvez A, Valdivia E, Maqueda M, Cruz V, Albert A, J Mol Biol. 2003 Nov 28;334(3):541-9. PMID:14623193
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- Enterococcus faecalis
- Single protein
- Albert, A.
- Cruz, V.
- Galvez, A.
- Maqueda, M.
- Martinez-Bueno, M.
- Martinez-Ripoll, M.
- Sanchez-Barrena, M.J.
- GOL
- SO4
- Bacteriocin
- Cationic antibacterial peptides
- Cyclic polypeptide
- Membrane permeabilization
- Protein crystallography
- Protein membrane interaction