Structure of the Enterococcus faecalis EIIA PTS component |
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Authors: | Stefan Reinelt Brigitte Koch Wolfgang Hengstenberg Klaus Scheffzek |
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Institution: | a European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany b AG Physiology of Microorganisms, Ruhr-Universitaet Bochum, 44780 Bochum, Germany |
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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 EIIAgnt component of the so far little investigated Enterococcus faecalis gluconate specific PTS. The crystal structure shows a tightly interacting dimer of EIIAgnt which is structurally similar to the related EIIAman from Escherichia coli. Homology modeling of E. faecalis HPr, EIIBman and their complexes with EIIAman suggests that despite moderate sequence identity between EIIAman and EIIAgnt, the active sites closely match the situation observed in the E. coli system with His-9 of EIIAgnt being the likely phosphoryl group carrier. We therefore propose that the phosphoryl transfer reactions involving EIIAgnt proceed according to a mechanism analog to the one described for E. coli EIIAman. |
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Keywords: | Enterococcus faecalis EIIA Phosphotransferase system X-ray Mannose Histidine Sugar Import Phosphoenolepyruvate EIIB |
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