4LT6

Crystal Structure of human poly(A) polymerase gamma

Summary for 4LT6

• Entry DOI: 10.2210/pdb4lt6/pdb
• Descriptor: Poly(A) polymerase gamma, 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: poly(a) polymerase, pap, polymerase, polyadenylation, 3' processing, mrna processing, nucleus, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9BWT3
• Total number of polymer chains: 2
• Total formula weight: 119641.90

Authors

Yang, Q.,Nausch, L.,Martin, G.,Keller, W.,Doublie, S. (deposition date: 2013-07-23, release date: 2013-10-09, Last modification date: 2023-09-20)

Primary citation

Yang, Q.,Nausch, L.W.,Martin, G.,Keller, W.,Doublie, S.
Crystal structure of human poly(a) polymerase gamma reveals a conserved catalytic core for canonical poly(a) polymerases.
J.Mol.Biol., 426:43-50, 2014

PubMed Abstract: In eukaryotes, the poly(A) tail added at the 3' end of an mRNA precursor is essential for the regulation of mRNA stability and the initiation of translation. Poly(A) polymerase (PAP) is the enzyme that catalyzes the poly(A) addition reaction. Multiple isoforms of PAP have been identified in vertebrates, which originate from gene duplication, alternative splicing or post-translational modifications. The complexity of PAP isoforms suggests that they might play different roles in the cell. Phylogenetic studies indicate that vertebrate PAPs are grouped into three clades termed α, β and γ, which originated from two gene duplication events. To date, all the available PAP structures are from the PAPα clade. Here, we present the crystal structure of the first representative of the PAPγ clade, human PAPγ bound to cordycepin triphosphate (3'dATP) and Ca(2+). The structure revealed that PAPγ closely resembles its PAPα ortholog. An analysis of residue conservation reveals a conserved catalytic binding pocket, whereas residues at the surface of the polymerase are more divergent.

PubMed: 24076191
DOI: 10.1016/j.jmb.2013.09.025

Experimental method

X-RAY DIFFRACTION (2.79 Å)