1f5a

CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE

spinqualitylabelsall models 1f5a, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1f5a is a 1 chain structure with sequence from Bos taurus. The October 2008 RCSB PDB Molecule of the Month feature on Poly(A) Polymerase by David Goodsell is 10.2210/rcsb_pdb/mom_2008_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3AT, 3PO, MN NonStd Res: MSE Activity: Polynucleotide adenylyltransferase, with EC number 2.7.7.19 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PAPOA_BOVIN] Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed In eukaryotes, polyadenylation of pre-mRNA plays an essential role in the initiation step of protein synthesis, as well as in the export and stability of mRNAs. Poly(A) polymerase, the enzyme at the heart of the polyadenylation machinery, is a template-independent RNA polymerase which specifically incorporates ATP at the 3' end of mRNA. We have solved the crystal structure of bovine poly(A) polymerase bound to an ATP analog at 2.5 A resolution. The structure revealed expected and unexpected similarities to other proteins. As expected, the catalytic domain of poly(A) polymerase shares substantial structural homology with other nucleotidyl transferases such as DNA polymerase beta and kanamycin transferase. The C-terminal domain unexpectedly folds into a compact domain reminiscent of the RNA-recognition motif fold. The three invariant aspartates of the catalytic triad ligate two of the three active site metals. One of these metals also contacts the adenine ring. Furthermore, conserved, catalytically important residues contact the nucleotide. These contacts, taken together with metal coordination of the adenine base, provide a structural basis for ATP selection by poly(A) polymerase. Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP.,Martin G, Keller W, Doublie S EMBO J. 2000 Aug 15;19(16):4193-203. PMID:10944102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Poly(A) Polymerase

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