3IPR

Crystal structure of the Enterococcus faecalis gluconate specific EIIA phosphotransferase system component

3IPR の概要

• エントリーDOI: 10.2210/pdb3ipr/pdb
• 分子名称: PTS system, IIA component, CALCIUM ION (3 entities in total)
• 機能のキーワード: 4 stranded parallel beta-sheet flanked by 3 alpha-helices on each side, transferase
• 由来する生物種: Enterococcus faecalis
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 95192.51

構造登録者

Reinelt, S.,Welti, S.,Scheffzek, K. (登録日: 2009-08-18, 公開日: 2009-09-15, 最終更新日: 2023-09-06)

主引用文献

Reinelt, S.,Koch, B.,Hothorn, M.,Hengstenberg, W.,Welti, S.,Scheffzek, K.
Structure of the Enterococcus faecalis EIIA(gnt) PTS component.
Biochem.Biophys.Res.Commun., 388:626-629, 2009

PubMed Abstract: In Eubacteria, the utilization of a number of extracellular carbohydrates is mediated by sugar specific phosphoenolepyruvate (PEP) dependent sugar phosphotransferase systems (PTSs), which simultaneously import und phosphorylate their target sugars. Here, we report the crystal structure of the EIIA(gnt) component of the so far little investigated Enterococcus faecalis gluconate specific PTS. The crystal structure shows a tightly interacting dimer of EIIA(gnt) which is structurally similar to the related EIIA(man) from Escherichia coli. Homology modeling of E. faecalis HPr, EIIB(man) and their complexes with EIIA(man) suggests that despite moderate sequence identity between EIIA(man) and EIIA(gnt), the active sites closely match the situation observed in the E. coli system with His-9 of EIIA(gnt) being the likely phosphoryl group carrier. We therefore propose that the phosphoryl transfer reactions involving EIIA(gnt) proceed according to a mechanism analog to the one described for E. coli EIIA(man).

PubMed: 19682976
DOI: 10.1016/j.bbrc.2009.08.054

実験手法

X-RAY DIFFRACTION (2.5 Å)