1go6
From Proteopedia
(New page: 200px<br /><applet load="1go6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1go6, resolution 0.98Å" /> '''BALHIMYCIN IN COMPLE...) |
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| - | [[Image:1go6.jpg|left|200px]]<br /><applet load="1go6" size=" | + | [[Image:1go6.jpg|left|200px]]<br /><applet load="1go6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1go6, resolution 0.98Å" /> | caption="1go6, resolution 0.98Å" /> | ||
'''BALHIMYCIN IN COMPLEX WITH LYS-D-ALA-D-ALA'''<br /> | '''BALHIMYCIN IN COMPLEX WITH LYS-D-ALA-D-ALA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The vancomycin-related antibiotics balhimycin and degluco-balhimycin have | + | 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== | ==About this Structure== | ||
| - | 1GO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with BMY, CIT, MRD and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1GO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=BMY:'>BMY</scene>, <scene name='pdbligand=CIT:'>CIT</scene>, <scene name='pdbligand=MRD:'>MRD</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GO6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bunkoczi, G.]] | [[Category: Bunkoczi, G.]] | ||
[[Category: Lehmann, C.]] | [[Category: Lehmann, C.]] | ||
| - | [[Category: Sheldrick, G | + | [[Category: Sheldrick, G M.]] |
[[Category: Vertesy, L.]] | [[Category: Vertesy, L.]] | ||
[[Category: BMY]] | [[Category: BMY]] | ||
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[[Category: vancomycin]] | [[Category: vancomycin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:12 2008'' |
Revision as of 10:52, 21 February 2008
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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] with , , and 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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