5X8R
Structure of the 30S small subunit of chloroplast ribosome from spinach
5X8R の概要
| エントリーDOI | 10.2210/pdb5x8r/pdb |
| EMDBエントリー | 6710 |
| 分子名称 | 30S ribosomal protein S2, chloroplastic, 30S ribosomal protein S12, chloroplastic, 30S ribosomal protein S13, chloroplastic, ... (26 entities in total) |
| 機能のキーワード | cryo-em, ribosome, chloroplast ribosome |
| 由来する生物種 | Spinacia oleracea (Spinach) 詳細 |
| タンパク質・核酸の鎖数 | 26 |
| 化学式量合計 | 913917.71 |
| 構造登録者 | |
| 主引用文献 | Ahmed, T.,Shi, J.,Bhushan, S. Unique localization of the plastid-specific ribosomal proteins in the chloroplast ribosome small subunit provides mechanistic insights into the chloroplastic translation Nucleic Acids Res., 45:8581-8595, 2017 Cited by PubMed Abstract: Chloroplastic translation is mediated by a bacterial-type 70S chloroplast ribosome. During the evolution, chloroplast ribosomes have acquired five plastid-specific ribosomal proteins or PSRPs (cS22, cS23, bTHXc, cL37 and cL38) which have been suggested to play important regulatory roles in translation. However, their exact locations on the chloroplast ribosome remain elusive due to lack of a high-resolution structure, hindering our progress to understand their possible roles. Here we present a cryo-EM structure of the 70S chloroplast ribosome from spinach resolved to 3.4 Å and focus our discussion mainly on the architecture of the 30S small subunit (SSU) which is resolved to 3.7 Å. cS22 localizes at the SSU foot where it seems to compensate for the deletions in 16S rRNA. The mRNA exit site is highly remodeled due to the presence of cS23 suggesting an alternative mode of translation initiation. bTHXc is positioned at the SSU head and appears to stabilize the intersubunit bridge B1b during thermal fluctuations. The translation factor plastid pY binds to the SSU on the intersubunit side and interacts with the conserved nucleotide bases involved in decoding. Most of the intersubunit bridges are conserved compared to the bacteria, except for a new bridge involving uL2c and bS6c. PubMed: 28582576DOI: 10.1093/nar/gkx499 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.7 Å) |
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