3AQK: Structure Of Bacterial Protein (apo Form I)

PolyA polymerase (PAP) adds a polyA tail onto the 3'-end of RNAs without a nucleic acid template, using adenosine-5'-triphosphate (ATP) as a substrate. The mechanism for the substrate selection by eubacterial PAP remains obscure. Structural and biochemical studies of Escherichia coli PAP (EcPAP) revealed that the shape and size of the nucleobase-interacting pocket of EcPAP are maintained by an intra-molecular hydrogen-network, making it suitable for the accommodation of only ATP, using a single amino acid, Arg(197). The pocket structure is sustained by interactions between the catalytic domain and the RNA-binding domain. EcPAP has a flexible basic C-terminal region that contributes to optimal RNA translocation for processive adenosine 5'-monophosphate (AMP) incorporations onto the 3'-end of RNAs. A comparison of the EcPAP structure with those of other template-independent RNA polymerases suggests that structural changes of domain(s) outside the conserved catalytic core domain altered the substrate specificities of the template-independent RNA polymerases.
PDB ID: 3AQKDownload
MMDB ID: 88476
PDB Deposition Date: 2010/11/9
Updated in MMDB: 2013/08
Experimental Method:
x-ray diffraction
Resolution: 3.65  Å
Source Organism:
Similar Structures:
Biological Unit for 3AQK: monomeric; determined by author and by software (PISA)
Molecular Components in 3AQK
Label Count Molecule
Protein (1 molecule)
Poly(a) Polymerase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB