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Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.

Ko TP, Huang CH, Lai SJ, Chen Y
Acta Crystallogr F Struct Biol Commun 74 765-769 (2018)
Cited: 4 times
EuropePMC logo PMID: 30511669

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 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 AbUPPS.

Articles - 6acs mentioned but not cited (3)

  1. Structural Characterization of Full-Length Human Dehydrodolichyl Diphosphate Synthase Using an Integrative Computational and Experimental Approach. Lisnyansky Bar-El M, Lee SY, Ki AY, Kapelushnik N, Loewenstein A, Chung KY, Schneidman-Duhovny D, Giladi M, Newman H, Haitin Y. Biomolecules 9 E660 (2019)
  2. Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii. Ko TP, Huang CH, Lai SJ, Chen Y. Acta Crystallogr F Struct Biol Commun 74 765-769 (2018)
  3. Cocktailed fragment screening by X-ray crystallography of the antibacterial target undecaprenyl pyrophosphate synthase from Acinetobacter baumannii. Thorpe JH, Wall ID, Sinnamon RH, Taylor AN, Stavenger RA. Acta Crystallogr F Struct Biol Commun 76 40-46 (2020)


Articles citing this publication (1)

  1. Investigations into the Antibacterial Mechanism of Action of Viridicatumtoxins. Li W, Li L, Zhang C, Cai Y, Gao Q, Wang F, Cao Y, Lin J, Li J, Shang Z, Lin W. ACS Infect Dis 6 1759-1769 (2020)


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