6CB2

Crystal structure of Escherichia coli UppP

Summary for 6CB2

• Entry DOI: 10.2210/pdb6cb2/pdb
• Descriptor: Undecaprenyl-diphosphatase, SULFATE ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total)
• Functional Keywords: undecaprenyl, pyrophosphate, phosphatase, hydrolase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 34121.98

Authors

Workman, S.D.,Worrall, L.J.,Strynadka, N.C.J. (deposition date: 2018-02-01, release date: 2018-03-28, Last modification date: 2024-03-13)

Primary citation

Workman, S.D.,Worrall, L.J.,Strynadka, N.C.J.
Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.
Nat Commun, 9:1159-1159, 2018

PubMed Abstract: Undecaprenyl pyrophosphate phosphatase (UppP) is an integral membrane protein that recycles the lipid carrier essential to the ongoing biosynthesis of the bacterial cell wall. Individual building blocks of peptidoglycan are assembled in the cytoplasm on undecaprenyl phosphate (C55-P) before being flipped to the periplasmic face, where they are polymerized and transferred to the existing cell wall sacculus, resulting in the side product undecaprenyl pyrophosphate (C55-PP). Interruption of UppP's regeneration of C55-P from C55-PP leads to the buildup of cell wall intermediates and cell lysis. We present the crystal structure of UppP from Escherichia coli at 2.0 Å resolution, which reveals the mechanistic basis for intramembranal phosphatase action and substrate specificity using an inverted topology repeat. In addition, the observation of key structural motifs common to a variety of cross membrane transporters hints at a potential flippase function in the specific relocalization of the C55-P product back to the cytosolic space.

PubMed: 29559664
DOI: 10.1038/s41467-018-03547-8

Experimental method

X-RAY DIFFRACTION (2 Å)