6ACS

poly-cis-prenyltransferase

Summary for 6ACS

• Entry DOI: 10.2210/pdb6acs/pdb
• Descriptor: Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific), CITRIC ACID, ISOPROPYL ALCOHOL, ... (5 entities in total)
• Functional Keywords: citrate, complex, undecaprenyl pyrophosphate, synthase, upps, transferase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 60209.88

Authors

Ko, T.-P.,Chen, Y. (deposition date: 2018-07-27, release date: 2018-12-19, Last modification date: 2023-11-22)

Primary citation

Ko, T.P.,Huang, C.H.,Lai, S.J.,Chen, Y.
Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii
Acta Crystallogr F Struct Biol Commun, 74:765-769, 2018

PubMed 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.

PubMed: 30511669
DOI: 10.1107/S2053230X18012931

Experimental method

X-RAY DIFFRACTION (1.81 Å)