Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins
Autore:
Fedorov, R; Meshcheryakov, V; Gongadze, G; Fomenkova, N; Nevskaya, N; Selmer, M; Laurberg, M; Kristensen, O; Al-Karadaghi, S; Liljas, A; Garber, M; Nikonov, S;
Indirizzi:
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142290 cow Region, Russia Univ Lund, Ctr Chem & Chem Engn, SE-22100 Lund, Sweden Univ Lund Lund Sweden SE-22100 r Chem & Chem Engn, SE-22100 Lund, Sweden
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 7
pagine: 968 - 976
SICI:
0907-4449(200107)57:<968:SORPTC>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-DENSITY MAPS; THERMUS-THERMOPHILUS; ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE; TERMINAL DOMAIN; NMR STRUCTURE; L25; RECOGNITION; POLYMERASE; MOLSCRIPT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Nikonov, S Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142290 Russia
Citazione:
R. Fedorov et al., "Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins", ACT CRYST D, 57, 2001, pp. 968-976

Abstract

The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3Angstrom resolution. The protein consists of two domains. The structure ofthe N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven beta -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules inthe asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:10:25