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Structure of balhimycin and its complex with solvent molecules

M Schäfer1, G M Sheldrick, T R Schneider

  • 1Institut für Anorganische Chemie der Universität Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany.

Acta Crystallographica. Section D, Biological Crystallography
|October 8, 1998
PubMed
Summary

Balhimycin, a glycopeptide antibiotic, forms dimers in crystals through hydrogen bonds. Its structure was solved using molecular replacement, revealing binding pockets occupied by citrate and acetate ions.

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Area of Science:

  • Biochemistry
  • Crystallography
  • Structural Biology

Background:

  • Balhimycin is a naturally occurring glycopeptide antibiotic.
  • It is structurally related to vancomycin.
  • It inhibits bacterial cell-wall synthesis by targeting the D-Ala-D-Ala peptide terminus.

Purpose of the Study:

  • To determine the crystal structure of balhimycin.
  • To elucidate the molecular interactions and assembly of balhimycin in the crystalline state.

Main Methods:

  • Crystallization of balhimycin.
  • X-ray diffraction data collection using synchrotron radiation.
  • Molecular replacement method for structure solution.
  • Anisotropic refinement of the crystal structure.

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Main Results:

  • The crystal structure of balhimycin was determined to a resolution of 0.96-45 A.
  • The asymmetric unit contains four independent balhimycin molecules, solvent molecules, citrate, and acetate ions.
  • Balhimycin monomers form dimers via antiparallel hydrogen bonds.
  • Each dimer exhibits binding pockets occupied by citrate and acetate ions.

Conclusions:

  • The crystal structure provides insights into the self-assembly of balhimycin.
  • The observed dimer formation and ion binding may be relevant to its biological activity.
  • The structural data contributes to understanding glycopeptide antibiotic mechanisms.