Journal article
Structure of ristocetin A in complex with a bacterial cell-wall mimetic
Acta crystallographica. Section D, Biological crystallography., v 65(Pt 8), pp 832-838
01 Aug 2009
PMID: 19622867
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The crystal structure of the complex between ristocetin A and the cell-wall peptide mimetic
N
-acetyl-lysine-
d
-alanine-
d
-alanine has been solved. Structural details explaining the anticooperativity of the antibiotic have been identified.
Antimicrobial drug resistance is a serious public health problem and the development of new antibiotics has become an important priority. Ristocetin A is a class III glycopeptide antibiotic that is used in the diagnosis of von Willebrand disease and which has served as a lead compound for the development of new antimicrobial therapeutics. The 1.0 Å resolution crystal structure of the complex between ristocetin A and a bacterial cell-wall peptide has been determined. As is observed for most other glycopeptide antibiotics, it is shown that ristocetin A forms a back-to-back dimer containing concave binding pockets that recognize the cell-wall peptide. A comparison of the structure of ristocetin A with those of class I glycopeptide antibiotics such as vancomycin and balhimycin identifies differences in the details of dimerization and ligand binding. The structure of the ligand-binding site reveals a likely explanation for ristocetin A’s unique anticooperativity between dimerization and ligand binding.
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Details
- Title
- Structure of ristocetin A in complex with a bacterial cell-wall mimetic
- Creators
- Virginie Nahoum - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102Sherri Spector - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102Patrick J Loll - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102
- Publication Details
- Acta crystallographica. Section D, Biological crystallography., v 65(Pt 8), pp 832-838
- Publisher
- International Union of Crystallography
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000268136800012
- Scopus ID
- 2-s2.0-68349143061
- Other Identifier
- 991014878437304721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemical Research Methods
- Biochemistry & Molecular Biology
- Biophysics
- Crystallography