Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-018-03477-5
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Funding
- Science Foundation Ireland [12/IA/1255]
- Federal Office for Scientific Technical and Cultural Affairs (IAP) [P7/44]
- FRS-FNRS [MIS F.4518.12, IISN 4.4503.11]
- Tournesol/Hubert Curien partnership between Belgium and France [R.CFRA.1567]
- Agence Nationale de la Recherche [ANR-11-BSV3-002]
- Centre National de la Recherche Scientifique
- University of Paris-Sud [UMR 9198]
- Deutsche Forschungsgemeinschaft (German Research Foundation)
- Wellcome Trust
- BBSRC [BB/I019855/1, BB/P01948X/1, BB/R002517/1]
- BBSRC [BB/R002517/1, BB/S003339/1, BB/P01948X/1, BB/I019855/1] Funding Source: UKRI
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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 angstrom 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.
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