4qs2

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'''Unreleased structure'''
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==70S ribosome translocation intermediate containing elongation factor EFG/GDP/fusidic acid, mRNA, and tRNAs trapped in the AP/AP pe/e chimeric hybrid state. This entry contains the 30S ribosomal subunit B. The 50S subunit B can be found in 4QS3. Molecule A in the same asymmetric unit is deposited as 4QS0 (30S) and 4QS1 (50S)==
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<StructureSection load='4qs2' size='340' side='right' caption='[[4qs2]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4qs2]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QS2 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUA:FUSIDIC+ACID'>FUA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMY:NEOMYCIN'>NMY</scene><br>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qs0|4qs0]], [[4qs1|4qs1]], [[4qs3|4qs3]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qs2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qs2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qs2 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Coupled translocation of messenger RNA and transfer RNA (tRNA) through the ribosome, a process catalyzed by elongation factor EF-G, is a crucial step in protein synthesis. The crystal structure of a bacterial translocation complex describes the binding states of two tRNAs trapped in mid-translocation. The deacylated P-site tRNA has moved into a partly translocated pe/E chimeric hybrid state. The anticodon stem-loop of the A-site tRNA is captured in transition toward the 30S P site, while its 3' acceptor end contacts both the A and P loops of the 50S subunit, forming an ap/ap chimeric hybrid state. The structure shows how features of ribosomal RNA rearrange to hand off the A-site tRNA to the P site, revealing an active role for ribosomal RNA in the translocation process.
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The entry 4qs2 is ON HOLD
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How the ribosome hands the A-site tRNA to the P site during EF-G-catalyzed translocation.,Zhou J, Lancaster L, Donohue JP, Noller HF Science. 2014 Sep 5;345(6201):1188-91. doi: 10.1126/science.1255030. PMID:25190797<ref>PMID:25190797</ref>
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Authors: Zhou, J., Lancaster, L., Donohue, J.P., Noller, H.F.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Small subunit of complex B
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Thermus thermophilus]]
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[[Category: Donohue, J P.]]
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[[Category: Lancaster, L.]]
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[[Category: Noller, H F.]]
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[[Category: Zhou, J.]]
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[[Category: Chimeric hybrid state ribosome]]
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[[Category: Ef-g]]
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[[Category: Mrna]]
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[[Category: Ribosome]]
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[[Category: Ribosome-antibiotic complex]]
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[[Category: Translocation 2 intermediate]]
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[[Category: Trna]]

Revision as of 00:16, 2 October 2014

70S ribosome translocation intermediate containing elongation factor EFG/GDP/fusidic acid, mRNA, and tRNAs trapped in the AP/AP pe/e chimeric hybrid state. This entry contains the 30S ribosomal subunit B. The 50S subunit B can be found in 4QS3. Molecule A in the same asymmetric unit is deposited as 4QS0 (30S) and 4QS1 (50S)

4qs2, resolution 3.80Å

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