4w2h

Crystal structure of the Thermus thermophilus 70S ribosome in complex with pactamycin (co-crystallized), mRNA and deacylated tRNA in the P site

spinqualitylabelsall models 4w2h, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4w2h is a 20 chain structure with sequence from Escherichia coli, Thermus thermophilus HB8 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: 4SU, 5MC, 5MU, 7MG, K, MG, MIA, PCY, PSU, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS18_THET8 Located on the back of the platform of the 30S subunit where it stabilizes the close packing of several RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome, where it probably interacts with the Shine-Dalgarno helix.[HAMAP-Rule:MF_00270] Publication Abstract from PubMed 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 A 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. Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome.,Polikanov YS, Osterman IA, Szal T, Tashlitsky VN, Serebryakova MV, Kusochek P, Bulkley D, Malanicheva IA, Efimenko TA, Efremenkova OV, Konevega AL, Shaw KJ, Bogdanov AA, Rodnina MV, Dontsova OA, Mankin AS, Steitz TA, Sergiev PV Mol Cell. 2014 Nov 20;56(4):531-40. doi: 10.1016/j.molcel.2014.09.020. Epub 2014 , Oct 9. PMID:25306919 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein THX 3D structures Ribosome 3D structures Transfer RNA (tRNA)

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