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Structure of the Enterococcus faecalis EIIA(gnt) PTS component.

Stefan Reinelt¹, Brigitte Koch, Michael Hothorn

¹European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

Biochemical and Biophysical Research Communications

|August 18, 2009

Summary

Researchers elucidated the structure of Enterococcus faecalis gluconate-specific phosphoenolpyruvate-dependent sugar phosphotransferase systems (PTSs). This reveals a mechanism for sugar import and phosphorylation similar to related systems in E. coli.

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Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

Area of Science:

Microbiology
Structural Biology
Biochemistry

Background:

Extracellular carbohydrate utilization in Eubacteria often involves phosphoenolpyruvate (PEP)-dependent sugar phosphotransferase systems (PTSs).
These systems simultaneously import and phosphorylate target sugars.
The Enterococcus faecalis gluconate-specific PTS, EIIA(gnt), was previously under-investigated.

Purpose of the Study:

To determine the crystal structure of the EIIA(gnt) component of the Enterococcus faecalis gluconate-specific PTS.
To compare its structure and potential mechanism with related PTS components from other bacteria, such as E. coli.

Main Methods:

X-ray crystallography was used to determine the structure of E. faecalis EIIA(gnt).
Homology modeling was employed to study E. faecalis HPr, EIIB(man), and their complexes with EIIA(man).
Structural comparisons were made between E. faecalis EIIA(gnt) and E. coli EIIA(man).

Main Results:

The crystal structure revealed EIIA(gnt) exists as a tightly interacting dimer.
EIIA(gnt) is structurally similar to EIIA(man) from Escherichia coli.
Despite moderate sequence identity, the active sites of EIIA(gnt) and EIIA(man) show close similarities, with His-9 in EIIA(gnt) identified as the probable phosphoryl group carrier.

Conclusions:

The structural and homology modeling data suggest a conserved mechanism for phosphoryl transfer in gluconate-specific PTSs.
The findings propose that EIIA(gnt) functions analogously to E. coli EIIA(man) in phosphoryl transfer reactions.
This study provides structural insights into a previously under-investigated bacterial PTS component.