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Titolo:
Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry
Autore:
Renault, L; Kerjan, P; Pasqualato, S; Menetrey, J; Robinson, JC; Kawaguchi, S; Vassylyev, DG; Yokoyama, S; Mirande, M; Cherfils, J;
Indirizzi:
CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France CNRS Gif Sur Yvette France F-91198 truct, F-91198 Gif Sur Yvette, France RIKEN, Harima Inst, Mikazuki, Hyogo 6795148, Japan RIKEN Mikazuki Hyogo Japan 6795148 a Inst, Mikazuki, Hyogo 6795148, Japan
Titolo Testata:
EMBO JOURNAL
fascicolo: 3, volume: 20, anno: 2001,
pagine: 570 - 578
SICI:
0261-4189(20010201)20:3<570:SOTEDO>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFER-RNA-SYNTHETASE; ACTIVATING POLYPEPTIDE-II; METHIONYL-TRANSFER-RNA; THERMUS-THERMOPHILUS; CRYSTAL-STRUCTURE; PROTEIN INTERACTIONS; EXTREME THERMOPHILE; BINDING DOMAINS; CYTOKINE; RECOGNITION;
Keywords:
aminoacyl-tRNA synthetase complex; convergent evolution; crystal structure; cytokine; EMAPII;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Cherfils, J CNRS, Lab Enzymol & Biochim Struct, 1 Ave Terrasse, F-91198 Gif Sur Yvette, France CNRS 1 Ave Terrasse Gif Sur Yvette France F-91198 tte, France
Citazione:
L. Renault et al., "Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry", EMBO J, 20(3), 2001, pp. 570-578

Abstract

The EMAPII (endothelial monocyte-activating polypeptide II) domain is a tRNA-binding domain associated with several aminoacyl-tRNA synthetases, whichbecomes an independent domain with inflammatory cytokine activity upon apoptotic cleavage from the p43 component of the multisynthetase complex, It comprises a domain that is highly homologous to bacterial tRNA-binding proteins (Trbp), followed by an extra domain without homology to known proteins,Trbps, which may represent ancient tRNA chaperones, form dimers and bind one tRNA per dimer, In contrast, EMAPII domains are monomers, Here we reportthe crystal structure at 1.14 Angstrom of human EMAPII, The structure reveals that the Trbp-like domain, which forms an oligonucleotide-binding (OB) fold, is related by degenerate 2-fold symmetry to the extra-domain. The pseudo-axis coincides with the dyad axis of bacterial TtCsaA, a Trbp whose structure was solved recently. The interdomain interface in EMAPII mimics the intersubunit interface in TtCsaA, and may thus generate a novel OB-fold-based tRNA-binding site. The low sequence homology between the extra domain ofEMAPII and either its own OB fold or that of Trbps suggests that dimer mimicry originated from convergent evolution rather than gene duplication.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 22:34:17