3OTO

Crystal Structure of the 30S ribosomal subunit from a KsgA mutant of Thermus thermophilus (HB8)

3OTO の概要

• エントリーDOI: 10.2210/pdb3oto/pdb
• 関連するPDBエントリー: 1j5e
• 分子名称: 16S rRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (24 entities in total)
• 機能のキーワード: 30s ribosomal subunit, ksga knock-out, post transcriptional rrna modification, antibiotic resistance, decoding, decoding of genetic code, trna, mrna, ribosome
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 787725.60

構造登録者

Demirci, H.,Murphy IV, F.,Belardinelli, R.,Kelley, A.C.,Ramakrishnan, V.,Gregory, S.T.,Dahlberg, A.E.,Jogl, G. (登録日: 2010-09-13, 公開日: 2010-09-29, 最終更新日: 2024-11-20)

主引用文献

Demirci, H.,Murphy, F.,Belardinelli, R.,Kelley, A.C.,Ramakrishnan, V.,Gregory, S.T.,Dahlberg, A.E.,Jogl, G.
Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function.
Rna, 16:2319-2324, 2010

PubMed Abstract: All organisms incorporate post-transcriptional modifications into ribosomal RNA, influencing ribosome assembly and function in ways that are poorly understood. The most highly conserved modification is the dimethylation of two adenosines near the 3' end of the small subunit rRNA. Lack of these methylations due to deficiency in the KsgA methyltransferase stimulates translational errors during both the initiation and elongation phases of protein synthesis and confers resistance to the antibiotic kasugamycin. Here, we present the X-ray crystal structure of the Thermus thermophilus 30S ribosomal subunit lacking these dimethylations. Our data indicate that the KsgA-directed methylations facilitate structural rearrangements in order to establish a functionally optimum subunit conformation during the final stages of ribosome assembly.

PubMed: 20962038
DOI: 10.1261/rna.2357210

実験手法

X-RAY DIFFRACTION (3.69 Å)