1o84

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[[Image:1o84.jpg|left|200px]]
[[Image:1o84.jpg|left|200px]]
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{{Structure
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|PDB= 1o84 |SIZE=350|CAPTION= <scene name='initialview01'>1o84</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1o84", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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{{STRUCTURE_1o84| PDB=1o84 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o84 OCA], [http://www.ebi.ac.uk/pdbsum/1o84 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o84 RCSB]</span>
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'''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.'''
'''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.'''
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[[Category: Sanchez-Barrena, M J.]]
[[Category: Sanchez-Barrena, M J.]]
[[Category: Valdivia, E.]]
[[Category: Valdivia, E.]]
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[[Category: antibacterial peptide]]
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[[Category: Antibacterial peptide]]
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[[Category: bacteriocin]]
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[[Category: Bacteriocin]]
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[[Category: cyclic polypeptide]]
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[[Category: Cyclic polypeptide]]
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[[Category: membrane permeabilization]]
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[[Category: Membrane permeabilization]]
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[[Category: protein crystallography]]
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[[Category: Protein crystallography]]
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[[Category: protein membrane interaction]]
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[[Category: Protein membrane interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:30:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:41:15 2008''
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Revision as of 00:30, 3 May 2008

Image:1o84.jpg

Template:STRUCTURE 1o84

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. 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 Sat May 3 03:30:22 2008

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