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; Martin Caffrey

doi:10.1038/s41467-018-03477-5

Nature Communications (Mar 2018)

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,
Martin Caffrey

Affiliations

Meriem El Ghachi: Centre d’Ingénierie des Protéines, InBioS, Université de Liège
Nicole Howe: Membrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin
Chia-Ying Huang: Membrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin
Vincent Olieric: Swiss Light Source, Paul Scherrer Institute
Rangana Warshamanage: Swiss Light Source, Paul Scherrer Institute
Thierry Touzé: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay
Dietmar Weichert: Membrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin
Phillip J. Stansfeld: Department of Biochemistry, University of Oxford
Meitian Wang: Swiss Light Source, Paul Scherrer Institute
Fred Kerff: Centre d’Ingénierie des Protéines, InBioS, Université de Liège
Martin Caffrey: Membrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College Dublin

DOI: https://doi.org/10.1038/s41467-018-03477-5
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 13

Abstract

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Bacterial cell wall components are assembled in a transmembrane cycle that involves the membrane integral pyrophosphorylase, BacA. Here the authors solve the crystal structure of BacA which shows an interdigitated inverted topology repeat that hints towards a flippase function for BacA.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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