6XHS

Crystal structure of S. aureus TarI in complex with CTP (space group P1211)

6XHS の概要

• エントリーDOI: 10.2210/pdb6xhs/pdb
• 分子名称: Ribitol-5-phosphate cytidylyltransferase 1, CYTIDINE-5'-TRIPHOSPHATE, THIOCYANATE ION, ... (5 entities in total)
• 機能のキーワード: cytidylyltransferase, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 175900.03

構造登録者

Li, F.K.K.,Strynadka, N.C.J. (登録日: 2020-06-19, 公開日: 2021-04-21, 最終更新日: 2023-10-18)

主引用文献

Li, F.K.K.,Gale, R.T.,Petrotchenko, E.V.,Borchers, C.H.,Brown, E.D.,Strynadka, N.C.J.
Crystallographic analysis of TarI and TarJ, a cytidylyltransferase and reductase pair for CDP-ribitol synthesis in Staphylococcus aureus wall teichoic acid biogenesis.
J.Struct.Biol., 213:107733-107733, 2021

PubMed Abstract: The cell wall of many pathogenic Gram-positive bacteria contains ribitol-phosphate wall teichoic acid (WTA), a polymer that is linked to virulence and regulation of essential physiological processes including cell division. CDP-ribitol, the activated precursor for ribitol-phosphate polymerization, is synthesized by a cytidylyltransferase and reductase pair known as TarI and TarJ, respectively. In this study, we present crystal structures of Staphylococcus aureus TarI and TarJ in their apo forms and in complex with substrates and products. The TarI structures illustrate the mechanism of CDP-ribitol synthesis from CTP and ribitol-phosphate and reveal structural changes required for substrate binding and catalysis. Insights into the upstream step of ribulose-phosphate reduction to ribitol-phosphate is provided by the structures of TarJ. Furthermore, we propose a general topology of the enzymes in a heterotetrameric form built using restraints from crosslinking mass spectrometry analysis. Together, our data present molecular details of CDP-ribitol production that may aid in the design of inhibitors against WTA biosynthesis.

PubMed: 33819634
DOI: 10.1016/j.jsb.2021.107733

実験手法

X-RAY DIFFRACTION (2.9 Å)