3AQL

Structure of bacterial protein (apo form II)

Summary for 3AQL

• Entry DOI: 10.2210/pdb3aql/pdb
• Related: 3AQK 3AQM 3AQN
• Descriptor: Poly(A) polymerase, MAGNESIUM ION, GLYCEROL (3 entities in total)
• Functional Keywords: transferase/rna, atp-binding, nucleotide-binding, rna-binding, transferase, nucleotidyltransferase, atp binding, a-phosphorylation
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 96263.02

Authors

Toh, Y.,Takeshita, D.,Tomita , K. (deposition date: 2010-11-09, release date: 2011-02-09, Last modification date: 2024-03-13)

Primary citation

Toh, Y.,Takeshita, D.,Nagaike, T.,Numata, T.,Tomita, K.
Mechanism for the alteration of the substrate specificities of template-independent RNA polymerases
Structure, 19:232-243, 2011

PubMed Abstract: 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.

PubMed: 21300291
DOI: 10.1016/j.str.2010.12.006

Experimental method

X-RAY DIFFRACTION (3 Å)