1BXY

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.

1BXY の概要

• エントリーDOI: 10.2210/pdb1bxy/pdb
• 分子名称: PROTEIN (RIBOSOMAL PROTEIN L30) (2 entities in total)
• 機能のキーワード: ribosomal protein, conformational changes, ribosome
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13598.25

構造登録者

Fedorov, R.,Nevskaya, N.,Khairullina, A.,Tishchenko, S.,Mikhailov, A.,Garber, M.,Nikonov, S. (登録日: 1998-10-09, 公開日: 1998-10-14, 最終更新日: 2024-02-07)

主引用文献

Fedorov, R.,Nevskaya, N.,Khairullina, A.,Tishchenko, S.,Mikhailov, A.,Garber, M.,Nikonov, S.
Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 A resolution: conformational flexibility of the molecule.
Acta Crystallogr.,Sect.D, 55:1827-1833, 1999

PubMed Abstract: The crystal structure of ribosomal protein L30 from the extreme thermophilic bacterium Thermus thermophilus has been determined at 1. 9 A resolution. The crystals are trigonal and belong to space group P3(2)21, with unit-cell parameters a = b = 63.5, c = 77.8 A, alpha = beta = 90, gamma = 120 degrees and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with X-PLOR to an R value of 20.3% and an R(free) of 25.3% in the resolution range 8-1.9 A. Detailed analyses of the structures of the two molecules in the asymmetric unit and comparison of T. thermophilus L30 structure with the structure of homologous L30 from Bacillus stearothermophilus reveal two flexible regions at opposite ends of the rather elongated molecule. Such flexibility could be important for the protein fitting in the ribosome. A comparison with B. stearothermophilus L30 shows a higher number of salt bridges and unbound positively charged residues and an increased accessible hydrophobic area on the surface of T. thermophilus L30. This could contribute to the stability of both the extreme thermophile protein and the ribosome as a whole.

PubMed: 10531479
DOI: 10.1107/S0907444999010227

実験手法

X-RAY DIFFRACTION (1.9 Å)