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1o82
From Proteopedia
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| - | [[Image:1o82.jpg|left|200px]] | + | [[Image:1o82.jpg|left|200px]] |
| - | + | ||
| - | '''X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF BACTERIOCIN AS-48 AT PH 4.5. SULPHATE BOUND FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O82 is a [ | + | 1O82 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O82 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14623193 14623193] |
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: bacteriocin]] | [[Category: bacteriocin]] | ||
| - | [[Category: cationic antibacterial | + | [[Category: cationic antibacterial peptide]] |
[[Category: cyclic polypeptide]] | [[Category: cyclic polypeptide]] | ||
[[Category: membrane permeabilization]] | [[Category: membrane permeabilization]] | ||
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[[Category: protein membrane interaction]] | [[Category: protein membrane interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:07:04 2008'' |
Revision as of 11:07, 20 March 2008
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| , resolution 1.46Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| 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 Thu Mar 20 13:07:04 2008
Categories: Enterococcus faecalis | Single protein | Albert, A. | Cruz, V. | Galvez, A. | Maqueda, M. | Martinez-Bueno, M. | Martinez-Ripoll, M. | Sanchez-Barrena, M J. | GOL | SO4 | Bacteriocin | Cationic antibacterial peptide | Cyclic polypeptide | Membrane permeabilization | Protein crystallography | Protein membrane interaction
