1MIY

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

Summary for 1MIY

• Entry DOI: 10.2210/pdb1miy/pdb
• Related: 1MIV 1MIW
• Descriptor: tRNA CCA-adding enzyme, MAGNESIUM ION, CYTIDINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: cca-adding enzyme, trna nucleotidyltransferase, translation, transferase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 2
• Total formula weight: 91930.08

Authors

Li, F.,Xiong, Y.,Wang, J.,Cho, H.D.,Weiner, A.M.,Steitz, T.A. (deposition date: 2002-08-23, release date: 2002-12-13, Last modification date: 2024-02-14)

Primary citation

Li, F.,Xiong, Y.,Wang, J.,Cho, H.D.,Tomita, K.,Weiner, A.M.,Steitz, T.A.
Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP
Cell(Cambridge,Mass.), 111:815-824, 2002

PubMed Abstract: 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.

PubMed: 12526808
DOI: 10.1016/S0092-8674(02)01115-7

Experimental method

X-RAY DIFFRACTION (3.52 Å)