1o82

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[[Image:1o82.jpg|left|200px]]
[[Image:1o82.jpg|left|200px]]
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{{Structure
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|PDB= 1o82 |SIZE=350|CAPTION= <scene name='initialview01'>1o82</scene>, resolution 1.46&Aring;
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The line below this paragraph, containing "STRUCTURE_1o82", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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{{STRUCTURE_1o82| PDB=1o82 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o82 OCA], [http://www.ebi.ac.uk/pdbsum/1o82 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o82 RCSB]</span>
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'''X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM'''
'''X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM'''
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[[Category: Martinez-Ripoll, M.]]
[[Category: Martinez-Ripoll, M.]]
[[Category: Sanchez-Barrena, M J.]]
[[Category: Sanchez-Barrena, M J.]]
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[[Category: bacteriocin]]
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[[Category: Bacteriocin]]
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[[Category: cationic antibacterial peptide]]
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[[Category: Cationic antibacterial peptide]]
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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 03:30:14 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:1o82.jpg

Template:STRUCTURE 1o82

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 Page seeded by OCA on Sat May 3 03:30:14 2008

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