1w3m: Difference between revisions
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==Overview== | ==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, . | 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== | ||
1W3M is a | 1W3M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_friuliensis Actinoplanes friuliensis] with CA, CL and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W3M OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: lipopetide]] | [[Category: lipopetide]] | ||
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Revision as of 11:20, 5 November 2007
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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 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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