1o84
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1O84 is a | + | 1O84 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with MAL, SO4, D10 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: GOL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O84 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein membrane interaction]] | [[Category: protein membrane interaction]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:00:23 2007'' |
Revision as of 11:55, 5 November 2007
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CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.
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
1O84 is a Single protein structure of sequence from Enterococcus faecalis with MAL, SO4, D10 and GOL as ligands. Structure known Active Site: GOL. 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
Page seeded by OCA on Mon Nov 5 14:00:23 2007
Categories: Enterococcus faecalis | Single protein | Albert, A. | Cruz, V. | Galvez, A. | Maqueda, M. | Martinez-Ripoll, M. | Sanchez-Barrena, M.J. | Valdivia, E. | D10 | GOL | MAL | SO4 | Antibacterial peptide | Bacteriocin | Cyclic polypeptide | Membrane permeabilization | Protein crystallography | Protein membrane interaction
