3uo0

phosphorylated Bacillus cereus phosphopentomutase soaked with glucose 1,6-bisphosphate

spinqualitylabelsall models 3uo0, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3uo0 is a 3 chain structure with sequence from Atcc 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: G16, MN, TRS NonStd Res: TPO Related: 3tx0, 3twz, 3un2, 3un3, 3un5, 3uny Gene: deoB, BC_4087 (ATCC 14579) Activity: Phosphopentomutase, with EC number 5.4.2.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DEOB_BACCR] Phosphotransfer between the C1 and C5 carbon atoms of pentose (By similarity). Publication Abstract from PubMed Prokaryotic phosphopentomutases (PPMs) are di-Mn(2+) enzymes that catalyze the interconversion of alpha-d-ribose 5-phosphate and alpha-d-ribose 1-phosphate at an active site located between two independently folded domains. These prokaryotic PPMs belong to the alkaline phosphatase superfamily, but previous studies of Bacillus cereus PPM suggested adaptations of the conserved alkaline phosphatase catalytic cycle. Notably, B. cereus PPM engages substrates when the active site nucleophile, Thr-85, is phosphorylated. Further, the phosphoenzyme is stable throughout purification and crystallization. In contrast, alkaline phosphatase engages substrates when the active site nucleophile is dephosphorylated, and the phosphoenzyme reaction intermediate is only stably trapped in a catalytically compromised enzyme. Studies were undertaken to understand the divergence of these mechanisms. Crystallographic and biochemical investigations of the PPM(T85E) phosphomimetic variant and the neutral corollary PPM(T85Q) determined that the side chain of Lys-240 underwent a change in conformation in response to active site charge, which modestly influenced the affinity for the small molecule activator alpha-d-glucose 1,6-bisphosphate. More strikingly, the structure of unphosphorylated B. cereus PPM revealed a dramatic change in the interdomain angle and a new hydrogen bonding interaction between the side chain of Asp-156 and the active site nucleophile, Thr-85. This hydrogen bonding interaction is predicted to align and activate Thr-85 for nucleophilic addition to alpha-d-glucose 1,6-bisphosphate, favoring the observed equilibrium phosphorylated state. Indeed, phosphorylation of Thr-85 is severely impaired in the PPM(D156A) variant even under stringent activation conditions. These results permit a proposal for activation of PPM and explain some of the essential features that distinguish between the catalytic cycles of PPM and alkaline phosphatase. Molecular Differences between a Mutase and a Phosphatase: Investigations of the Activation Step in Bacillus cereus Phosphopentomutase.,Iverson TM, Panosian TD, Birmingham WR, Nannemann DP, Bachmann BO Biochemistry. 2012 Feb 21. PMID:22329805 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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