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Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
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El Ghachi, Meriem, Howe, Nicole, Huang, Chia-Ying, Olieric, Vincent, Warshamanage, Rangana, Touzé, Thierry, Weichert, Dietmar, Stansfeld, Phillip J., Wang, Meitian, Kerff, Fred and Caffrey, Martin (2018) Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nature Communications, 9 (1). 1078 . doi:10.1038/s41467-018-03477-5
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WRAP-crystal-structure-undecaprenyl-pyrophosphate-biosynsthesis-Stansfeld-2018.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2540Kb) | Preview |
Official URL: http://dx.doi.org/10.1038/s41467-018-03477-5
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.
| Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||||||||
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| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology Q Science > QR Microbiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||||||||||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Peptidoglycans, Pyrophosphates, Phosphatases, Biosynthesis, Crystals -- Structure | ||||||||||||||||||||||||||||||||||||||||||
| Journal or Publication Title: | Nature Communications | ||||||||||||||||||||||||||||||||||||||||||
| Publisher: | Nature Publishing Group | ||||||||||||||||||||||||||||||||||||||||||
| ISSN: | 2041-1723 | ||||||||||||||||||||||||||||||||||||||||||
| Official Date: | 14 March 2018 | ||||||||||||||||||||||||||||||||||||||||||
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| Volume: | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Number: | 1 | ||||||||||||||||||||||||||||||||||||||||||
| Article Number: | 1078 | ||||||||||||||||||||||||||||||||||||||||||
| DOI: | 10.1038/s41467-018-03477-5 | ||||||||||||||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||||||||||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||||||||||||||||||||||||||
| Access rights to Published version: | Open Access | ||||||||||||||||||||||||||||||||||||||||||
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