1go6
From Proteopedia
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|PDB= 1go6 |SIZE=350|CAPTION= <scene name='initialview01'>1go6</scene>, resolution 0.98Å | |PDB= 1go6 |SIZE=350|CAPTION= <scene name='initialview01'>1go6</scene>, resolution 0.98Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BMY:BALHIMYCIN'>BMY</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BMY:BALHIMYCIN'>BMY</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1go6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1go6 OCA], [http://www.ebi.ac.uk/pdbsum/1go6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1go6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
[[Category: Vertesy, L.]] | [[Category: Vertesy, L.]] | ||
| - | [[Category: BMY]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: MRD]] | ||
[[Category: bacterial cell-wall]] | [[Category: bacterial cell-wall]] | ||
[[Category: glycopeptide antibiotic]] | [[Category: glycopeptide antibiotic]] | ||
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[[Category: vancomycin]] | [[Category: vancomycin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:01 2008'' |
Revision as of 17:48, 30 March 2008
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| , resolution 0.98Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BALHIMYCIN IN COMPLEX WITH LYS-D-ALA-D-ALA
Overview
The vancomycin-related antibiotics balhimycin and degluco-balhimycin have been crystallized in complexes with di-, tri- and pentapeptides that emulate bacterial cell-wall precursors, and four structures determined at atomic resolution (<1 A). In addition to the features expected from previous structural and spectroscopic studies, two new motifs were observed that may prove important in the design of antibiotics modified to overcome bacterial resistance. A changed binding mode was found in two dipeptide complexes, and a new type of face-to-face oligomerization (in addition to the well-established back-to-back dimerization) was seen when the model peptide reaches a critical fraction of the size of the cell-wall precursor pentapeptide. The extensive interactions involving both antibiotic and peptide molecules in this interface should appreciably enhance the kinetic and thermodynamic stability of the complexes. In the pentapeptide complex, the relative positions of the peptides are close to those required for d-Ala elimination, so this structure may provide a realistic model for the prevention of the enzyme-catalyzed cell-wall crosslinking by antibiotic binding.
About this Structure
1GO6 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structures of glycopeptide antibiotics with peptides that model bacterial cell-wall precursors., Lehmann C, Bunkoczi G, Vertesy L, Sheldrick GM, J Mol Biol. 2002 May 3;318(3):723-32. PMID:12054818
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