1o83: Difference between revisions
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[[Image:1o83. | [[Image:1o83.jpg|left|200px]]<br /><applet load="1o83" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1o83" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1o83, resolution 1.64Å" /> | caption="1o83, resolution 1.64Å" /> | ||
'''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48 AT PH 7.5, PHOSPHATE BOUND. CRYSTAL FORM I'''<br /> | '''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48 AT PH 7.5, PHOSPHATE BOUND. CRYSTAL FORM I'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1O83 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 PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. | 1O83 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 PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Po4 Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O83 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein membrane interaction]] | [[Category: protein membrane interaction]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:00:34 2007'' | ||
Revision as of 14:50, 18 December 2007
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CRYSTAL STRUCTURE OF BACTERIOCIN AS-48 AT PH 7.5, PHOSPHATE BOUND. CRYSTAL FORM I
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
1O83 is a Single protein structure of sequence from Enterococcus faecalis with PO4 and GOL as ligands. Known structural/functional Site: AC1. 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
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