1O82: X-Ray Structure Of Bacteriocin As-48 At Ph 4.5. Sulphate Bound Form

Citation:
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.
PDB ID: 1O82Download
MMDB ID: 25281
PDB Deposition Date: 2002/11/22
Updated in MMDB: 2003/12
Experimental Method:
x-ray diffraction
Resolution: 1.46  Å
Source Organism:
Similar Structures:
Biological Unit for 1O82: monomeric; determined by author and by software (PQS)
Molecular Components in 1O82
Label Count Molecule
Protein (1 molecule)
1
Peptide Antibiotic As-48
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.