3H38: The Structure Of Cca-adding Enzyme Apo Form Ii

Citation:
Abstract
The CCA-adding enzyme synthesizes the CCA sequence at the 3' end of tRNA without a nucleic acid template. The crystal structures of class II Thermotoga maritima CCA-adding enzyme and its complexes with CTP or ATP were determined. The structure-based replacement of both the catalytic heads and nucleobase-interacting neck domains of the phylogenetically closely related Aquifex aeolicus A-adding enzyme by the corresponding domains of the T. maritima CCA-adding enzyme allowed the A-adding enzyme to add CCA in vivo and in vitro. However, the replacement of only the catalytic head domain did not allow the A-adding enzyme to add CCA, and the enzyme exhibited (A, C)-adding activity. We identified the region in the neck domain that prevents (A, C)-adding activity and defines the number of nucleotide incorporations and the specificity for correct CCA addition. We also identified the region in the head domain that defines the terminal A addition after CC addition. The results collectively suggest that, in the class II CCA-adding enzyme, the head and neck domains collaboratively and dynamically define the number of nucleotide additions and the specificity of nucleotide selection.
PDB ID: 3H38Download
MMDB ID: 77305
PDB Deposition Date: 2009/4/16
Updated in MMDB: 2009/10
Experimental Method:
x-ray diffraction
Resolution: 2.37  Å
Source Organism:
Similar Structures:
Biological Unit for 3H38: monomeric; determined by author and by software (PISA)
Molecular Components in 3H38
Label Count Molecule
Protein (1 molecule)
1
tRNA Nucleotidyl Transferase-related Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.