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Titolo:
Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP
Autore:
Martin, G; Keller, W; Doublie, S;
Indirizzi:
Univ Basel, Bioctr, Dept Cell Biol, CH-4056 Basel, Switzerland Univ BaselBasel Switzerland CH-4056 ll Biol, CH-4056 Basel, Switzerland Univ Vermont, Dept Microbiol & Mol Genet, Markey Ctr Mol Genet, Burlington, VT 05405 USA Univ Vermont Burlington VT USA 05405 Mol Genet, Burlington, VT 05405 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 16, volume: 19, anno: 2000,
pagine: 4193 - 4203
SICI:
0261-4189(20000815)19:16<4193:CSOMPP>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RNA POLYADENYLATION; MULTIPLE ISOMORPHOUS REPLACEMENT; DNA-POLYMERASE; POLY(A)-BINDING PROTEIN; SPECIFICITY FACTOR; NUCLEOTIDYLTRANSFERASE SUPERFAMILY; KANAMYCIN NUCLEOTIDYLTRANSFERASE; THERMUS-THERMOPHILUS; ANGSTROM RESOLUTION; MUTATIONAL ANALYSIS;
Keywords:
crystal structure; mRNA 3 ' end processing; phosphoryl transfer; poly(A) polymerase; terminal nucleotidyl transferase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
68
Recensione:
Indirizzi per estratti:
Indirizzo: Keller, W Univ Basel, Bioctr, Dept Cell Biol, Klingelbergstr 70, CH-4056 Basel, Switzerland Univ Basel Klingelbergstr 70 Basel Switzerland CH-4056 tzerland
Citazione:
G. Martin et al., "Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP", EMBO J, 19(16), 2000, pp. 4193-4203

Abstract

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 Angstrom resolution. The structure revealed expected and unexpected similarities to otherproteins. 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 motiffold. The three invariant aspartates of the catalytic triad ligate two of the three active site metals, One of these metals also contacts the adeninering. Furthermore, conserved, catalytically important residues contact thenucleotide, These contacts, taken together with metal coordination of the adenine base, provide a structural basis for ATP selection by poly(A) polymerase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 07:13:33