1w3m

From Proteopedia

Revision as of 15:19, 5 November 2007

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 CA, CL and EOH as ligands. Structure known Active Site: AC1. 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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