Unraveling a bacterial hexose transport pathway.
Structural information about proteins involved in bacterial hexose transport mediated by the phosphoenolpyruvate:sugar phosphotransferase system is rapidly accumulating. Within the past year, two crystal structures and two solution NMR structures of the histidine-containing phosphocarrier protein have been reported, adding structural details to previous NMR and crystallographic work on this protein and on enzyme IIA. The crystal structure of the regulatory complex between the glucose enzyme IIA and glycerol kinase has been determined, and the association of the histidine-containing phosphocarrier protein and either the glucose enzyme IIA or the mannitol enzyme IIA have been studied by NMR. Proposals concerning the mechanism of phosphoryl transfer and the protein-protein interactions involved may now be tested more rigorously using these data.
Herzberg
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O
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville 20850.
Klevit
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R
D001426:Bacterial Proteins; D005991:Glycerol Kinase / Q000737:chemistry / Q000378:metabolism; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
D001426:Bacterial Proteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; D005991:Glycerol Kinase