1w3m: Difference between revisions

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[[Image:1w3m.gif|left|200px]]
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{{STRUCTURE_1w3m|  PDB=1w3m  |  SCENE=  }}  
{{STRUCTURE_1w3m|  PDB=1w3m  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF TSUSHIMYCIN'''
===CRYSTAL STRUCTURE OF TSUSHIMYCIN===




==Overview==
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The amphomycin derivative tsushimycin has been crystallized and its structure determined at 1.0 A resolution. The asymmetric unit contains 12 molecules and with 1300 independent atoms this structure is one of the largest solved using ab initio direct methods. The antibiotic is comprised of a cyclodecapeptide core, an exocyclic amino acid and a fatty-acid residue. Its backbone adopts a saddle-like conformation that is stabilized by a Ca2+ ion bound within the peptide ring and accounts for the Ca2+-dependence of this antibiotic class. Additional Ca2+ ions link the antibiotic molecules to dimers that enclose an empty space resembling a binding cleft. The dimers possess a large hydrophobic surface capable of interacting with the bacterial cell membrane. The antibiotic daptomycin may exhibit a similar conformation, as the amino-acid sequence is conserved at positions involved in Ca2+ binding.
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==About this Structure==
==About this Structure==
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[[Category: Daptomycin]]
[[Category: Daptomycin]]
[[Category: Lipopetide]]
[[Category: Lipopetide]]
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Revision as of 20:43, 27 July 2008

File:1w3m.png

Template:STRUCTURE 1w3m

CRYSTAL STRUCTURE OF TSUSHIMYCIN

Template:ABSTRACT PUBMED 16041082

About this Structure

1W3M is a Single protein structure of sequence from Actinoplanes friuliensis. Full crystallographic information is available from OCA.

Reference

Structure of the lipopeptide antibiotic tsushimycin., Bunkoczi G, Vertesy L, Sheldrick GM, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1160-4. Epub 2005, Jul 20. PMID:16041082

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