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1o84
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The bacteriocin AS-48 is a membrane-interacting peptide, which displays 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== | ||
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[[Category: Maqueda, M.]] | [[Category: Maqueda, M.]] | ||
[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
| - | [[Category: Sanchez-Barrena, M | + | [[Category: Sanchez-Barrena, M J.]] |
[[Category: Valdivia, E.]] | [[Category: Valdivia, E.]] | ||
[[Category: D10]] | [[Category: D10]] | ||
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[[Category: protein membrane interaction]] | [[Category: protein membrane interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:31 2008'' |
Revision as of 12:14, 21 February 2008
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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 , , and 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
Page seeded by OCA on Thu Feb 21 14:14:31 2008
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
