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1w3m
From Proteopedia
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[[Image:1w3m.gif|left|200px]] | [[Image:1w3m.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF TSUSHIMYCIN''' | '''CRYSTAL STRUCTURE OF TSUSHIMYCIN''' | ||
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[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
[[Category: Vertesy, L.]] | [[Category: Vertesy, L.]] | ||
| - | [[Category: | + | [[Category: Amphomycin]] |
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Daptomycin]] |
| - | [[Category: | + | [[Category: Lipopetide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:06:44 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:06, 3 May 2008
CRYSTAL STRUCTURE OF TSUSHIMYCIN
Overview
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.
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 Page seeded by OCA on Sat May 3 13:06:44 2008
