Skip to Main content Skip to Navigation
Journal articles

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

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.
Document type :
Journal articles
Complete list of metadatas

https://hal-cea.archives-ouvertes.fr/cea-01876552
Contributor : Bruno Savelli <>
Submitted on : Tuesday, September 18, 2018 - 3:14:30 PM
Last modification on : Friday, September 11, 2020 - 3:17:59 AM

Links full text

Identifiers

Citation

Meriem El Ghachi, Nicole Howe, Chia-Ying Huang, Vincent Oliéric, Rangana Warshamanage, et al.. Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nature Communications, Nature Publishing Group, 2018, 9, pp.1078. ⟨10.1038/s41467-018-03477-5⟩. ⟨cea-01876552⟩

Share

Metrics

Record views

88