1miw
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1miw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1miw, resolution 3.00Å" /> '''Crystal structure of...)
Next diff →
Revision as of 19:19, 20 November 2007
|
Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP
Overview
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.
About this Structure
1MIW is a Single protein structure of sequence from Geobacillus stearothermophilus with MG and ATP as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 21:26:36 2007
