Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis

Meriem El Ghachi, Nicole Howe, Chia-Ying Huang, Vincent Olieric, Rangana Warshamanage, Thierry Touzé, Dietmar Weichert, Phillip J. Stansfeld, Meitian Wang, Fred Kerff and Martin Caffrey ()
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Meriem El Ghachi: Université de Liège
Nicole Howe: School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin
Chia-Ying Huang: School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin
Vincent Olieric: Paul Scherrer Institute
Rangana Warshamanage: Paul Scherrer Institute
Thierry Touzé: Université Paris-Sud, Université Paris-Saclay
Dietmar Weichert: School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin
Phillip J. Stansfeld: University of Oxford
Meitian Wang: Paul Scherrer Institute
Fred Kerff: Université de Liège
Martin Caffrey: School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: Abstract As a protective envelope surrounding the bacterial cell, the peptidoglycan sacculus is a site of vulnerability and an antibiotic target. Peptidoglycan components, assembled in the cytoplasm, are shuttled across the membrane in a cycle that uses undecaprenyl-phosphate. A product of peptidoglycan synthesis, undecaprenyl-pyrophosphate, is converted to undecaprenyl-phosphate for reuse in the cycle by the membrane integral pyrophosphatase, BacA. To understand how BacA functions, we determine its crystal structure at 2.6 Å resolution. The enzyme is open to the periplasm and to the periplasmic leaflet via a pocket that extends into the membrane. Conserved residues map to the pocket where pyrophosphorolysis occurs. BacA incorporates an interdigitated inverted topology repeat, a topology type thus far only reported in transporters and channels. This unique topology raises issues regarding the ancestry of BacA, the possibility that BacA has alternate active sites on either side of the membrane and its possible function as a flippase.

Date: 2018
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DOI: 10.1038/s41467-018-03477-5

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