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Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.


ABSTRACT: 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 (AbUPPS) 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 ?-sheet with several surrounding ?-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 AbUPPS.

SUBMITTER: Ko TP 

PROVIDER: S-EPMC6277960 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.

Ko Tzu Ping TP   Huang Chi Hung CH   Lai Shu Jung SJ   Chen Yeh Y  

Acta crystallographica. Section F, Structural biology communications 20181116 Pt 12


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 (AbUPPS) 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 surroundi  ...[more]

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