1GHG

CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON

Summary for 1GHG

• Entry DOI: 10.2210/pdb1ghg/pdb
• Related: 1AA5 1C0Q 1C0R 1FVM 1GAC 1PN3 1PNV 1QD8 1RRV 1SHO
• Related PRD ID: PRD_000206
• Descriptor: VANCOMYCIN AGLYCON, ACETIC ACID, DIMETHYL SULFOXIDE, ... (4 entities in total)
• Functional Keywords: glycopeptide, antibiotic, aglycon, vancomycin
• Biological source: AMYCOLATOPSIS ORIENTALIS
• Total number of polymer chains: 4
• Total formula weight: 4996.38

Authors

Kaplan, J.,Korty, B.D.,Axelsen, P.H.,Loll, P.J. (deposition date: 2000-12-13, release date: 2001-02-12, Last modification date: 2023-12-27)

Primary citation

Kaplan, J.,Korty, B.D.,Axelsen, P.H.,Loll, P.J.
The Role of Sugar Residues in Molecular Recognition by Vancomycin
J.Med.Chem., 44:1837-, 2001

PubMed Abstract: The sugar residues of the glycopeptide antibiotic vancomycin contribute to the cooperativity of ligand binding, thereby increasing ligand affinity and enhancing antimicrobial activity. To assess the structural basis for these effects, we determined a 0.98 A X-ray crystal structure of the vancomycin aglycon and compared it to structures of several intact vancomycin:ligand complexes. The crystal structure reveals that the aglycon binds acetate anions and forms back-to-back dimeric complexes in a manner similar to that of intact vancomycin. However, the four independent copies of the aglycon in each asymmetric unit of the crystal exhibit a high degree of conformational heterogeneity. These results suggest that the sugar residues, in addition to enlarging and strengthening the dimer interface, provide steric constraints that limit the vancomycin molecule to a relatively small number of productive conformations.

PubMed: 11356118
DOI: 10.1021/JM0005306

Experimental method

X-RAY DIFFRACTION (0.98 Å)