2xz7

CRYSTAL STRUCTURE OF THE PHOSPHOENOLPYRUVATE-BINDING DOMAIN OF ENZYME I IN COMPLEX WITH PHOSPHOENOLPYRUVATE FROM THE THERMOANAEROBACTER TENGCONGENSIS PEP-SUGAR PHOSPHOTRANSFERASE SYSTEM (PTS)

spinqualitylabelsall models 2xz7, resolution 1.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xz7 is a 1 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.83Å Ligands: MG, PEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8R7R4_CALS4 General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).[PIRNR:PIRNR000732] Publication Abstract from PubMed Thermoanaerobacter tengcongensis is a thermophilic eubacterium that has a phosphoenolpyruvate (PEP) sugar phosphotransferase system (PTS) of 22 proteins. The general PTS proteins, enzyme I and HPr, and the transporters for N-acetylglucosamine (EIICB(GlcNAc)) and fructose (EIIBC(Fru)) have thermal unfolding transitions at approximately 90 degrees C and a temperature optimum for in vitro sugar phosphotransferase activity of 65 degrees C. The phosphocysteine of a EIICB(GlcNAc) mutant is unusually stable at room temperature with a t(1/2) of 60 h. The PEP binding C-terminal domain of enzyme I (EIC) forms a metastable covalent adduct with PEP at 65 degrees C. Crystallization of this adduct afforded the 1.68 A resolution structure of EIC with a molecule of pyruvate in the active site. We also report the 1.83 A crystal structure of the EIC-PEP complex. The comparison of the two structures with the apo form and with full-length EI shows differences between the active site side chain conformations of the PEP and pyruvate states but not between the pyruvate and apo states. In the presence of PEP, Arg465 forms a salt bridge with the phosphate moiety while Glu504 forms salt bridges with Arg186 and Arg195 of the N-terminal domain of enzyme I (EIN), which stabilizes a conformation appropriate for the in-line transfer of the phosphoryl moiety from PEP to His191. After transfer, Arg465 swings 4.8 A away to form an alternative salt bridge with the carboxylate of Glu504. Glu504 loses the grip of Arg186 and Arg195, and the EIN domain can swing away to hand on the phosphoryl group to the phosphoryl carrier protein HPr. Phosphoenolpyruvate: sugar phosphotransferase system from the hyperthermophilic Thermoanaerobacter tengcongensis.,Navdaeva V, Zurbriggen A, Waltersperger S, Schneider P, Oberholzer AE, Bahler P, Bachler C, Grieder A, Baumann U, Erni B Biochemistry. 2011 Feb 22;50(7):1184-93. Epub 2011 Jan 20. PMID:21250658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase 3D structures

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