3lnw

Close correlation of protein thermostability and self-buried area rate revealed by crystal structure of HPr from Thermoanaerobacter tengcongensis MB4

spinqualitylabelsall models 3lnw, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lnw is a 3 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis MB4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.302Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8R910_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. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.[ARBA:ARBA00003681]

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