1w3m

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Revision as of 16:10, 29 October 2007

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spinqualitylabelsall models 1w3m, resolution 1.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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, ... [(full description)]

About this Structure

1W3M is a [Single protein] structure of sequence from [Actinoplanes friuliensis] with CA, CL and EOH as [ligands]. 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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