7yzn

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7yzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi_GE5 Pyrococcus abyssi GE5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YZN FirstGlance]. <br>
<table><tr><td colspan='2'>[[7yzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi_GE5 Pyrococcus abyssi GE5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YZN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yzn OCA], [https://pdbe.org/7yzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yzn RCSB], [https://www.ebi.ac.uk/pdbsum/7yzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yzn ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yzn OCA], [https://pdbe.org/7yzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yzn RCSB], [https://www.ebi.ac.uk/pdbsum/7yzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yzn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/IF2P_PYRAB IF2P_PYRAB]] Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
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[https://www.uniprot.org/uniprot/IF2P_PYRAB IF2P_PYRAB] Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In eukaryotes and in archaea late steps of translation initiation involve the two initiation factors e/aIF5B and e/aIF1A. In eukaryotes, the role of eIF5B in ribosomal subunit joining is established and structural data showing eIF5B bound to the full ribosome were obtained. To achieve its function, eIF5B collaborates with eIF1A. However, structural data illustrating how these two factors interact on the small ribosomal subunit have long been awaited. The role of the archaeal counterparts, aIF5B and aIF1A, remains to be extensively addressed. Here, we study the late steps of Pyrococcus abyssi translation initiation. Using in vitro reconstituted initiation complexes and light scattering, we show that aIF5B bound to GTP accelerates subunit joining without the need for GTP hydrolysis. We report the crystallographic structures of aIF5B bound to GDP and GTP and analyze domain movements associated to these two nucleotide states. Finally, we present the cryo-EM structure of an initiation complex containing 30S bound to mRNA, Met-tRNAiMet, aIF5B and aIF1A at 2.7 A resolution. Structural data shows how archaeal 5B and 1A factors cooperate to induce a conformation of the initiator tRNA favorable to subunit joining. Archaeal and eukaryotic features of late steps of translation initiation are discussed.
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Role of aIF5B in archaeal translation initiation.,Kazan R, Bourgeois G, Lazennec-Schurdevin C, Larquet E, Mechulam Y, Coureux PD, Schmitt E Nucleic Acids Res. 2022 Jun 24;50(11):6532-6548. doi: 10.1093/nar/gkac490. PMID:35694843<ref>PMID:35694843</ref>
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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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<div class="pdbe-citations 7yzn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of C-terminally truncated aIF5B from Pyrococcus abyssi complexed with GTP

PDB ID 7yzn

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