4U3N

Crystal structure of CCA trinucleotide bound to the yeast 80S ribosome

これはPDB形式変換不可エントリーです。

4U3N の概要

• エントリーDOI: 10.2210/pdb4u3n/pdb
• 分子名称: 18S ribosomal RNA, 40S ribosomal protein S8-A, 40S ribosomal protein S9-A, ... (91 entities in total)
• 機能のキーワード: translation, ribosome, 40s, 60s, 80s, eukaryote, rna-protein complex, inhibitor, antibiotic
• 由来する生物種: Saccharomyces cerevisiae ATCC 204508 / S288c; 詳細
• 細胞内の位置: Cytoplasm : P32905 P33442 P25443 P05750 P0CX35 P26783 P0CX37 P26786 P0CX39 O13516 Q08745 P0CX47 P48589 P05756 P06367 Q01855 P0CX51 P02407 P0CX55 P07280 P38701 P0C0V8 P0C0W1 P0CX29 P0CX31 Q3E792 P39939 P35997 Q3E7X9 P41057 P0CX33 P38011 P39015 P0CX45 P14126 P10664 P26321 Q02326 P05737 P17076 P05738 P41805 Q3E757 Q12690 P36105 P05748 P26784 P05740 P0CX49 P0CX82 P0CX23 Q02753 P05749 P0CX41 P04449 P04456 P05743 P0C2H6 P02406 P05747 P14120 P0C2H8 P38061 P05744 P87262 P0CX84 P05745 P49166 P49167 P04650 P0CX86 P0CX27 P0CX25 Q08745 P0CX33 P05317; Ubiquitin: Cytoplasm . 40S ribosomal protein S31: Cytoplasm : P05759 P05759; Ubiquitin: Cytoplasm . 60S ribosomal protein L40: Cytoplasm: P0CH08
• タンパク質・核酸の鎖数: 162
• 化学式量合計: 6632895.45

構造登録者

Garreau de Loubresse, N.,Prokhorova, I.,Yusupova, G.,Yusupov, M. (登録日: 2014-07-22, 公開日: 2014-10-22, 最終更新日: 2023-12-20)

主引用文献

Garreau de Loubresse, N.,Prokhorova, I.,Holtkamp, W.,Rodnina, M.V.,Yusupova, G.,Yusupov, M.
Structural basis for the inhibition of the eukaryotic ribosome.
Nature, 513:517-522, 2014

PubMed Abstract: The ribosome is a molecular machine responsible for protein synthesis and a major target for small-molecule inhibitors. Compared to the wealth of structural information available on ribosome-targeting antibiotics in bacteria, our understanding of the binding mode of ribosome inhibitors in eukaryotes is currently limited. Here we used X-ray crystallography to determine 16 high-resolution structures of 80S ribosomes from Saccharomyces cerevisiae in complexes with 12 eukaryote-specific and 4 broad-spectrum inhibitors. All inhibitors were found associated with messenger RNA and transfer RNA binding sites. In combination with kinetic experiments, the structures suggest a model for the action of cycloheximide and lactimidomycin, which explains why lactimidomycin, the larger compound, specifically targets the first elongation cycle. The study defines common principles of targeting and resistance, provides insights into translation inhibitor mode of action and reveals the structural determinants responsible for species selectivity which could guide future drug development.

PubMed: 25209664
DOI: 10.1038/nature13737

実験手法

X-RAY DIFFRACTION (3.2 Å)