1o82

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spinqualitylabelsall models 1o82, resolution 1.46Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 water-soluble, form to a membrane-bound state upon membrane binding.

About this Structure

1O82 is a Single protein structure of sequence from Enterococcus faecalis with SO4 and GOL as ligands. Known structural/functional Site: . 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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