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| {{STRUCTURE_1go6| PDB=1go6 | SCENE= }} | | {{STRUCTURE_1go6| PDB=1go6 | SCENE= }} |
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| '''BALHIMYCIN IN COMPLEX WITH LYS-D-ALA-D-ALA'''
| | ===BALHIMYCIN IN COMPLEX WITH LYS-D-ALA-D-ALA=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12054818}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12054818 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12054818}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Peptide complex]] | | [[Category: Peptide complex]] |
| [[Category: Vancomycin]] | | [[Category: Vancomycin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:48:43 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:35:35 2008'' |
