7otr | pdb_00007otr

Crystal structure of a psychrophilic CCA-adding enzyme determined by SAD phasing

spinqualitylabelsall models 7otr, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7otr is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, GOL, PO4, TRS Related: 6qy6, 6qxn Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A1C7DQ98_9BACL] Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.[SAAS:SAAS00711016] Publication Abstract from PubMed CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence C-C-A at tRNA 3'-ends. Recently, we could reveal that cold adaptation of such a polymerase is not only achieved at the expense of enzyme stability, but also at the cost of polymerization fidelity. Enzymes from psychrophilic organisms usually show an increased structural flexibility to enable catalysis at low temperatures. Here, polymerases face a dilemma, as there is a discrepancy between the need for a tightly controlled flexibility during polymerization and an increased flexibility as strategy for cold adaptation. Based on structural and biochemical analyses, we contribute to clarify the cold adaptation strategy of the psychrophilic CCA-adding enzyme from Planococcus halocryophilus, a gram-positive bacterium thriving in the arctic permafrost at low temperatures down to -15 degrees C. A comparison with the closely related enzyme from the thermophilic bacterium Geobacillus stearothermophilus reveals several features of cold adaptation - a significantly reduced amount of alpha-helical elements in the C-terminal tRNA-binding region and a structural adaptation in one of the highly conserved catalytic core motifs located in the N-terminal catalytic core of the enzyme. CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus.,de Wijn R, Rollet K, Ernst FGM, Wellner K, Betat H, Morl M, Sauter C Comput Struct Biotechnol J. 2021 Oct 21;19:5845-5855. doi:, 10.1016/j.csbj.2021.10.018. eCollection 2021. PMID:34765099 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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