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Structure of the Bacillus anthracis dTDP‐l‐rhamnose‐biosynthetic enzyme dTDP‐4‐dehydrorhamnose 3,5‐epimerase (RfbC)

Structure of the Bacillus anthracis dTDP‐l‐rhamnose‐biosynthetic enzyme dTDP‐4‐dehydrorhamnose... The exosporium layer of Bacillus anthracis spores is rich in l‐rhamnose, a common bacterial cell‐wall component, which often contributes to the virulence of pathogens by increasing their adherence and immune evasion. The biosynthetic pathway used to form the activated l‐rhamnose donor dTDP‐l‐rhamnose consists of four enzymes (RfbA, RfbB, RfbC and RfbD) and is an attractive drug target because there are no homologs in mammals. It was found that co‐purifying and screening RfbC (dTDP‐6‐deoxy‐d‐xylo‐4‐hexulose 3,5‐epimerase) from B. anthracis in the presence of the other three B. anthracis enzymes of the biosynthetic pathway yielded crystals that were suitable for data collection. RfbC crystallized as a dimer and its structure was determined at 1.63 Å resolution. Two different ligands were bound in the protein structure: pyrophosphate in the active site of one monomer and dTDP in the other monomer. A structural comparison with RfbC homologs showed that the key active‐site residues are conserved across kingdoms. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Structure of the Bacillus anthracis dTDP‐l‐rhamnose‐biosynthetic enzyme dTDP‐4‐dehydrorhamnose 3,5‐epimerase (RfbC)

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Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17015849
pmid
29199987
Publisher site
See Article on Publisher Site

Abstract

The exosporium layer of Bacillus anthracis spores is rich in l‐rhamnose, a common bacterial cell‐wall component, which often contributes to the virulence of pathogens by increasing their adherence and immune evasion. The biosynthetic pathway used to form the activated l‐rhamnose donor dTDP‐l‐rhamnose consists of four enzymes (RfbA, RfbB, RfbC and RfbD) and is an attractive drug target because there are no homologs in mammals. It was found that co‐purifying and screening RfbC (dTDP‐6‐deoxy‐d‐xylo‐4‐hexulose 3,5‐epimerase) from B. anthracis in the presence of the other three B. anthracis enzymes of the biosynthetic pathway yielded crystals that were suitable for data collection. RfbC crystallized as a dimer and its structure was determined at 1.63 Å resolution. Two different ligands were bound in the protein structure: pyrophosphate in the active site of one monomer and dTDP in the other monomer. A structural comparison with RfbC homologs showed that the key active‐site residues are conserved across kingdoms.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ; ;

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