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Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii
Author(s) -
Ko Tzu-Ping,
Huang Chi-Hung,
Lai Shu-Jung,
Chen Yeh
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18012931
Subject(s) - peptidoglycan , acinetobacter baumannii , pyrophosphate , atp synthase , biochemistry , chemistry , serine , transferase , stereochemistry , biology , enzyme , bacteria , genetics , pseudomonas aeruginosa
Undecaprenyl pyrophosphate (UPP) is an important carrier of the oligosaccharide component in peptidoglycan synthesis. Inhibition of UPP synthase (UPPS) may be an effective strategy in combating the pathogen Acinetobacter baumannii , which has evolved to be multidrug‐resistant. Here, A. baumannii UPPS ( Ab UPPS) was cloned, expressed, purified and crystallized, and its structure was determined by X‐ray diffraction. Each chain of the dimeric protein folds into a central β‐sheet with several surrounding α‐helices, including one at the C‐terminus. In the active site, two molecules of citrate interact with the side chains of the catalytic aspartate and serine. These observations may provide a structural basis for inhibitor design against Ab UPPS.