4lt6

Crystal Structure of human poly(A) polymerase gamma

spinqualitylabelsall models 4lt6, resolution 2.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lt6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.79Å Ligands: 3AT, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAPOG_HUMAN Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. Publication Abstract from PubMed 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 alpha, beta and gamma, which originated from two gene duplication events. To date, all the available PAP structures are from the PAPalpha clade. Here, we present the crystal structure of the first representative of the PAPgamma clade, human PAPgamma bound to cordycepin triphosphate (3'dATP) and Ca2+. The structure revealed that PAPgamma closely resembles its PAPalpha ortholog. An analysis of residue conservation reveals a conserved catalytic binding pocket, whereas residues at the surface of the polymerase are more divergent. Crystal Structure of Human Poly(A) Polymerase Gamma Reveals a Conserved Catalytic Core for Canonical Poly(A) Polymerases.,Yang Q, Nausch L, Martin G, Keller W, Doublie S J Mol Biol. 2013 Sep 25. pii: S0022-2836(13)00609-8. doi:, 10.1016/j.jmb.2013.09.025. PMID:24076191 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Poly(A) polymerase 3D structures

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