6CB2

Crystal structure of Escherichia coli UppP

6CB2 の概要

• エントリーDOI: 10.2210/pdb6cb2/pdb
• 分子名称: Undecaprenyl-diphosphatase, SULFATE ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total)
• 機能のキーワード: undecaprenyl, pyrophosphate, phosphatase, hydrolase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34121.98

構造登録者

Workman, S.D.,Worrall, L.J.,Strynadka, N.C.J. (登録日: 2018-02-01, 公開日: 2018-03-28, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)