1o82
From Proteopedia
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|PDB= 1o82 |SIZE=350|CAPTION= <scene name='initialview01'>1o82</scene>, resolution 1.46Å | |PDB= 1o82 |SIZE=350|CAPTION= <scene name='initialview01'>1o82</scene>, resolution 1.46Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
[[Category: Sanchez-Barrena, M J.]] | [[Category: Sanchez-Barrena, M J.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: bacteriocin]] | [[Category: bacteriocin]] | ||
[[Category: cationic antibacterial peptide]] | [[Category: cationic antibacterial peptide]] | ||
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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 Sun Mar 30 22:41:15 2008'' |
Revision as of 19:41, 30 March 2008
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| , resolution 1.46Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:41:15 2008
Categories: Enterococcus faecalis | Single protein | Albert, A. | Cruz, V. | Galvez, A. | Maqueda, M. | Martinez-Bueno, M. | Martinez-Ripoll, M. | Sanchez-Barrena, M J. | Bacteriocin | Cationic antibacterial peptide | Cyclic polypeptide | Membrane permeabilization | Protein crystallography | Protein membrane interaction
