1miw | pdb_00001miw

Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP

spinqualitylabelsall models 1miw, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1miw is a 2 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG NonStd Res: MSE Related: 1miv, 1miy Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed CCA-adding enzymes polymerize CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template. The 3.0 A resolution crystal structures of the CCA-adding enzyme from Bacillus stearothermophilus and its complexes with ATP or CTP reveal a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head is structurally homologous to the palm domain of DNA polymerase beta but has additional structural features and functions. The neck, body, and tail represent new protein folding motifs. The neck provides a specific template for the incoming ATP or CTP, whereas the body and tail may bind tRNA. Each subunit has one active site capable of switching its base specificity between ATP and CTP, an important component of the CCA-adding mechanism. Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.,Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA Cell. 2002 Dec 13;111(6):815-24. PMID:12526808 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CCA-adding enzyme

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