NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA

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DOIResolve DOI: http://doi.org/10.1110/ps.062337406
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TypeArticle
Journal titleProtein Science
Volume15
Issue10
Pages24352441; # of pages: 7
SubjectCarbohydrates; Cysteine; Escherichia coli; Molecular Weight; Multienzyme Complexes; pha; phosphatase; Phosphorylation; Protein; Protein-Tyrosine-Phosphatase; Tyrosine
AbstractThe phosphoenolpyruvate-dependent carbohydrate transport system (PTS) couples uptake with phosphorylation of a variety of carbohydrates in prokaryotes. In this multienzyme complex, the enzyme II (EII), a carbohydrate-specific permease, is constituted of two cytoplasmic domains, IIA and IIB, and a transmembrane channel IIC domain. Among the five families of EIIs identified in Escherichia coli, the galactitol-specific transporter (II(gat)) belongs to the glucitol family and is structurally the least well-characterized. Here, we used nuclear magnetic resonance (NMR) spectroscopy to solve the three-dimensional structure of the IIB subunit (GatB). GatB consists of a central four-stranded parallel beta-sheet flanked by alpha-helices on both sides; the active site cysteine of GatB is located at the beginning of an unstructured loop between beta1 and alpha1 that folds into a P-loop-like structure. This structural arrangement shows similarities with other IIB subunits but also with mammalian low molecular weight protein tyrosine phosphatases (LMW PTPase) and arsenate reductase (ArsC). An NMR titration was performed to identify the GatA-interacting residues
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AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47537
NPARC number3539657
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Record identifier7597a6e6-7e53-4378-abb4-6aaae0561ee4
Record created2009-03-01
Record modified2016-05-09
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