1w3m
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The amphomycin derivative tsushimycin has been crystallized and its | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bunkoczi, G.]] | [[Category: Bunkoczi, G.]] | ||
| - | [[Category: Sheldrick, G | + | [[Category: Sheldrick, G M.]] |
[[Category: Vertesy, L.]] | [[Category: Vertesy, L.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: lipopetide]] | [[Category: lipopetide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:09 2008'' |
Revision as of 13:40, 21 February 2008
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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 with , and as ligands. Known structural/functional Site: . 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 Thu Feb 21 15:40:09 2008
Categories: Actinoplanes friuliensis | Single protein | Bunkoczi, G. | Sheldrick, G M. | Vertesy, L. | CA | CL | EOH | Amphomycin | Antibiotic | Daptomycin | Lipopetide
