1hhu
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(New page: 200px<br /><applet load="1hhu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hhu, resolution 0.89Å" /> '''BALHIMYCIN IN COMPLE...)
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Revision as of 00:29, 25 November 2007
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BALHIMYCIN IN COMPLEX WITH 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
1HHU is a Protein complex structure of sequences from Amycolatopsis sp. with BMY, CIT and MPD as ligands. 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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