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