1hhu
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1hhu |SIZE=350|CAPTION= <scene name='initialview01'>1hhu</scene>, resolution 0.89Å | |PDB= 1hhu |SIZE=350|CAPTION= <scene name='initialview01'>1hhu</scene>, resolution 0.89Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BMY:BALHIMYCIN'>BMY</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene> | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhu OCA], [http://www.ebi.ac.uk/pdbsum/1hhu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hhu RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
[[Category: Vertessy, L.]] | [[Category: Vertessy, L.]] | ||
| - | [[Category: BMY]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: MPD]] | ||
[[Category: cell wall peptide]] | [[Category: cell wall peptide]] | ||
[[Category: direct method]] | [[Category: direct method]] | ||
| Line 34: | Line 34: | ||
[[Category: vacomycin]] | [[Category: vacomycin]] | ||
| - | ''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 21:05:11 2008'' |
Revision as of 18:05, 30 March 2008
| |||||||
| , resolution 0.89Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.. 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
Page seeded by OCA on Sun Mar 30 21:05:11 2008
