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Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
- Source :
- Nature Communications, Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018), Nature Communications, Nature Publishing Group, 2018, 9, pp.1078. ⟨10.1038/s41467-018-03477-5⟩, Nature Communications, 2018, 9, pp.1078. ⟨10.1038/s41467-018-03477-5⟩
- Publication Year :
- 2018
- Publisher :
- Nature Publishing Group, 2018.
-
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.<br />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.
- Subjects :
- 0301 basic medicine
Science
Molecular Sequence Data
General Physics and Astronomy
Peptidoglycan
Crystallography, X-Ray
Models, Biological
01 natural sciences
Article
Protein Structure, Secondary
General Biochemistry, Genetics and Molecular Biology
Bacterial cell structure
03 medical and health sciences
chemistry.chemical_compound
Polyisoprenyl Phosphates
0103 physical sciences
QD
Amino Acid Sequence
Pyrophosphatases
lcsh:Science
Multidisciplinary
010304 chemical physics
Escherichia coli Proteins
General Chemistry
Flippase
Periplasmic space
QP
Phosphoric Monoester Hydrolases
Cell biology
QR
A-site
030104 developmental biology
chemistry
Membrane protein
Structural biology
Cytoplasm
[SDV.IB]Life Sciences [q-bio]/Bioengineering
lcsh:Q
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Database :
- OpenAIRE
- Journal :
- Nature Communications, Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018), Nature Communications, Nature Publishing Group, 2018, 9, pp.1078. ⟨10.1038/s41467-018-03477-5⟩, Nature Communications, 2018, 9, pp.1078. ⟨10.1038/s41467-018-03477-5⟩
- Accession number :
- edsair.doi.dedup.....0661b1b254c938fdf4b7c43f99f884e5