5OON
Structure of Undecaprenyl-Pyrophosphate Phosphatase, BacA
Summary for 5OON
| Entry DOI | 10.2210/pdb5oon/pdb |
| Descriptor | Undecaprenyl-diphosphatase, MERCURY (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total) |
| Functional Keywords | antibiotic, bacterial cell wall, enzyme mechanism, escherichia coli, in meso in situ serial crystallography, imisx, interdigitated inverted topology repeat, lipid cubic phase, membrane protein, peptidoglycan, phosphatase, pyrophosphorylase, undecaprenyl-pyrophosphate |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 32124.28 |
| Authors | Huang, C.-Y.,Olieric, V.,Warshamanage, R.,Wang, M.,Howe, N.,Ghachi, M.E.I.,Weichert, D.,Kerff, F.,Stansfeld, P.,Touze, T.,Caffrey, M. (deposition date: 2017-08-08, release date: 2018-03-21, Last modification date: 2024-05-08) |
| Primary citation | El Ghachi, M.,Howe, N.,Huang, C.Y.,Olieric, V.,Warshamanage, R.,Touze, T.,Weichert, D.,Stansfeld, P.J.,Wang, M.,Kerff, F.,Caffrey, M. Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nat Commun, 9:1078-1078, 2018 Cited by PubMed 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. PubMed: 29540682DOI: 10.1038/s41467-018-03477-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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