5I4L
Crystal structure of Amicoumacin A bound to the yeast 80S ribosome
This is a non-PDB format compatible entry.
Summary for 5I4L
| Entry DOI | 10.2210/pdb5i4l/pdb |
| Descriptor | 18S ribosomal RNA, 40S ribosomal protein S8-A, 40S ribosomal protein S9-A, ... (89 entities in total) |
| Functional Keywords | ribosome, inhibitor |
| Biological source | Saccharomyces cerevisiae S288c More |
| Cellular location | Cytoplasm : P32905 P33442 P25443 P05750 P0CX35 P26783 P0CX37 P26786 P0CX39 O13516 Q08745 P0CX47 P48589 P05756 P39516 Q01855 P0CX51 P02407 P0CX55 P07280 P38701 P0C0V8 P0C0W1 P0CX29 P0CX31 Q3E792 P39939 P35997 Q3E7X9 P41057 P0CX33 P38011 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 P17076 P04449 P05317 Ubiquitin: Cytoplasm . 40S ribosomal protein S31: Cytoplasm : P05759 Ubiquitin: Cytoplasm . 60S ribosomal protein L40: Cytoplasm: P0CH08 |
| Total number of polymer chains | 162 |
| Total formula weight | 6467209.46 |
| Authors | Prokhorova, I.V.,Yusupova, G.,Yusupov, M. (deposition date: 2016-02-12, release date: 2016-06-22, Last modification date: 2024-05-08) |
| Primary citation | Prokhorova, I.V.,Akulich, K.A.,Makeeva, D.S.,Osterman, I.A.,Skvortsov, D.A.,Sergiev, P.V.,Dontsova, O.A.,Yusupova, G.,Yusupov, M.M.,Dmitriev, S.E. Amicoumacin A induces cancer cell death by targeting the eukaryotic ribosome. Sci Rep, 6:27720-27720, 2016 Cited by PubMed Abstract: Amicoumacin A is an antibiotic that was recently shown to target bacterial ribosomes. It affects translocation and provides an additional contact interface between the ribosomal RNA and mRNA. The binding site of amicoumacin A is formed by universally conserved nucleotides of rRNA. In this work, we showed that amicoumacin A inhibits translation in yeast and mammalian systems by affecting translation elongation. We determined the structure of the amicoumacin A complex with yeast ribosomes at a resolution of 3.1 Å. Toxicity measurement demonstrated that human cancer cell lines are more susceptible to the inhibition by this compound as compared to non-cancerous ones. This might be used as a starting point to develop amicoumacin A derivatives with clinical value. PubMed: 27296282DOI: 10.1038/srep27720 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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