1DD3

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 FROM THERMOTOGA MARITIMA

1DD3 の概要

• エントリーDOI: 10.2210/pdb1dd3/pdb
• 分子名称: 50S RIBOSOMAL PROTEIN L7/L12 (3 entities in total)
• 機能のキーワード: dimer formation, flexibility, hinge region, four-helix-bundle, five-helix- bundle, alpha-beta structure, helical hairpin, domains, ribosome
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 34171.42

構造登録者

Wahl, M.C.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R. (登録日: 1999-11-08, 公開日: 2000-11-13, 最終更新日: 2024-02-07)

主引用文献

Wahl, M.C.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R.
Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12.
EMBO J., 19:174-186, 2000

PubMed Abstract: Protein L12, the only multicopy component of the ribosome, is presumed to be involved in the binding of translation factors, stimulating factor-dependent GTP hydrolysis. Crystal structures of L12 from Thermotogamaritima have been solved in two space groups by the multiple anomalous dispersion method and refined at 2.4 and 2.0 A resolution. In both crystal forms, an asymmetric unit comprises two full-length L12 molecules and two N-terminal L12 fragments that are associated in a specific, hetero-tetrameric complex with one non-crystallographic 2-fold axis. The two full-length proteins form a tight, symmetric, parallel dimer, mainly through their N-terminal domains. Each monomer of this central dimer additionally associates in a different way with an N-terminal L12 fragment. Both dimerization modes are unlike models proposed previously and suggest that similar complexes may occur in vivo and in situ. The structures also display different L12 monomer conformations, in accord with the suggested dynamic role of the protein in the ribosomal translocation process. The structures have been submitted to the Protein Databank (http://www.rcsb.org/pdb) under accession numbers 1DD3 and 1DD4.

PubMed: 10637222
DOI: 10.1093/emboj/19.2.174

実験手法

X-RAY DIFFRACTION (2 Å)