4W2G

Crystal structure of the Thermus thermophilus 70S ribosome in complex with pactamycin (soaked), mRNA and three deacylated tRNAs in the A, P and E sites

これはPDB形式変換不可エントリーです。

4W2G の概要

• エントリーDOI: 10.2210/pdb4w2g/pdb
• 分子名称: 16S Ribosomal RNA, 30S Ribosomal Protein S10, 30S Ribosomal Protein S11, ... (61 entities in total)
• 機能のキーワード: pactamycin, antibiotic, 70s ribosome, inhibition of translation, initiation inhibitor, 30s subunit with pactamycin (soaked), mrna, deacylated a-, p-, and e-site trnas of the 1st 70s ribosome in the asu, functional complex of bacterial 70s ribosome with antibiotic pactamycin (compact conformation), 50s subunit of the 1st 70s ribosome in the asu, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 112
• 化学式量合計: 4554628.56

構造登録者

Polikanov, Y.S.,Osterman, I.A.,Szal, T.,Tashlitsky, V.N.,Serebryakova, M.V.,Kusochek, P.,Bulkley, D.,Malanicheva, I.A.,Efimenko, T.A.,Efremenkova, O.V.,Konevega, A.L.,Shaw, K.J.,Bogdanov, A.A.,Rodnina, M.V.,Dontsova, O.A.,Mankin, A.S.,Steitz, T.A.,Sergiev, P.V. (登録日: 2014-09-12, 公開日: 2014-10-15, 最終更新日: 2023-12-27)

主引用文献

Polikanov, Y.S.,Osterman, I.A.,Szal, T.,Tashlitsky, V.N.,Serebryakova, M.V.,Kusochek, P.,Bulkley, D.,Malanicheva, I.A.,Efimenko, T.A.,Efremenkova, O.V.,Konevega, A.L.,Shaw, K.J.,Bogdanov, A.A.,Rodnina, M.V.,Dontsova, O.A.,Mankin, A.S.,Steitz, T.A.,Sergiev, P.V.
Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome.
Mol.Cell, 56:531-540, 2014

PubMed Abstract: We demonstrate that the antibiotic amicoumacin A (AMI) is a potent inhibitor of protein synthesis. Resistance mutations in helix 24 of the 16S rRNA mapped the AMI binding site to the small ribosomal subunit. The crystal structure of bacterial ribosome in complex with AMI solved at 2.4 Å resolution revealed that the antibiotic makes contacts with universally conserved nucleotides of 16S rRNA in the E site and the mRNA backbone. Simultaneous interactions of AMI with 16S rRNA and mRNA and the in vivo experimental evidence suggest that it may inhibit the progression of the ribosome along mRNA. Consistent with this proposal, binding of AMI interferes with translocation in vitro. The inhibitory action of AMI can be partly compensated by mutations in the translation elongation factor G.

PubMed: 25306919
DOI: 10.1016/j.molcel.2014.09.020

実験手法

X-RAY DIFFRACTION (2.55 Å)