Structure of Ristocetin A in Complex with a Bacterial Cell-wall Mimetic

Overview

Journal Acta Crystallogr D Biol Crystallogr

Specialty Chemistry

Date 2009 Jul 23

PMID 19622867

Citations 9

Authors

Virginie Nahoum

Sherri Spector

Patrick J Loll

Affiliations

Soon will be listed here.

Abstract

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 A 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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