1w3m: Difference between revisions
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[[Image:1w3m.gif|left|200px]] | [[Image:1w3m.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF TSUSHIMYCIN''' | {{Structure | ||
|PDB= 1w3m |SIZE=350|CAPTION= <scene name='initialview01'>1w3m</scene>, resolution 1.00Å | |||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+C'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EOH:ETHANOL'>EOH</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF TSUSHIMYCIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1W3M is a [ | 1W3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_friuliensis Actinoplanes friuliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3M OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16041082 16041082] | ||
[[Category: Actinoplanes friuliensis]] | [[Category: Actinoplanes friuliensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipopetide]] | [[Category: lipopetide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:51:38 2008'' | ||
Revision as of 12:51, 20 March 2008
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| 1w3m, resolution 1.00Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CA, CL and EOH | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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