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Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.
- Source :
-
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2018 Dec 01; Vol. 74 (Pt 12), pp. 765-769. Date of Electronic Publication: 2018 Nov 16. - Publication Year :
- 2018
-
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.
- Subjects :
- Acinetobacter baumannii genetics
Alkyl and Aryl Transferases genetics
Amino Acid Sequence
Crystallization methods
Protein Structure, Secondary
Protein Structure, Tertiary
X-Ray Diffraction methods
Acinetobacter baumannii chemistry
Acinetobacter baumannii enzymology
Alkyl and Aryl Transferases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 2053-230X
- Volume :
- 74
- Issue :
- Pt 12
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Publication Type :
- Academic Journal
- Accession number :
- 30511669
- Full Text :
- https://doi.org/10.1107/S2053230X18012931