3IPR

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

Summary for 3IPR

• Entry DOI: 10.2210/pdb3ipr/pdb
• Descriptor: PTS system, IIA component, CALCIUM ION (3 entities in total)
• Functional Keywords: 4 stranded parallel beta-sheet flanked by 3 alpha-helices on each side, transferase
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 6
• Total formula weight: 95192.51

Authors

Reinelt, S.,Welti, S.,Scheffzek, K. (deposition date: 2009-08-18, release date: 2009-09-15, Last modification date: 2023-09-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)