1o84
From Proteopedia
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| - | [[Image:1o84.jpg|left|200px]]<br /><applet load="1o84" size=" | + | [[Image:1o84.jpg|left|200px]]<br /><applet load="1o84" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o84, resolution 2.8Å" /> | caption="1o84, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.'''<br /> | '''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O84 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with MAL, SO4, D10 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=GOL:So4 Binding Site For Chain B'>GOL</scene>. Full crystallographic information is available from [http:// | + | 1O84 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=D10:'>D10</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=GOL:So4+Binding+Site+For+Chain+B'>GOL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O84 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein membrane interaction]] | [[Category: protein membrane interaction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:54:44 2008'' |
Revision as of 07:54, 3 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 Sun Feb 3 09:54:44 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
