7uiu: Difference between revisions

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<StructureSection load='7uiu' size='340' side='right'caption='[[7uiu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='7uiu' size='340' side='right'caption='[[7uiu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7uiu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UIU FirstGlance]. <br>
<table><tr><td colspan='2'>[[7uiu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UIU FirstGlance]. <br>
</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=7uiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uiu OCA], [https://pdbe.org/7uiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uiu RCSB], [https://www.ebi.ac.uk/pdbsum/7uiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uiu ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</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=7uiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uiu OCA], [https://pdbe.org/7uiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uiu RCSB], [https://www.ebi.ac.uk/pdbsum/7uiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uiu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IF2_PSEAE IF2_PSEAE]] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.[HAMAP-Rule:MF_00100]  
[https://www.uniprot.org/uniprot/IF2_PSEAE IF2_PSEAE] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.[HAMAP-Rule:MF_00100]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During translation initiation, initiation factor 2 (IF2) holds initiator transfer RNA (fMet-tRNAi(fMet)) in a specific orientation in the peptidyl (P) site of the ribosome. Upon subunit joining IF2 hydrolyzes GTP and, concomitant with inorganic phosphate (Pi) release, changes conformation facilitating fMet-tRNAi(fMet) accommodation into the P site and transition of the 70 S ribosome initiation complex (70S-IC) to an elongation-competent ribosome. The mechanism by which IF2 separates from initiator tRNA at the end of translation initiation remains elusive. Here, we report cryo-electron microscopy (cryo-EM) structures of the 70S-IC from Pseudomonas aeruginosa bound to compact IF2-GDP and initiator tRNA. Relative to GTP-bound IF2, rotation of the switch 2 alpha-helix in the G-domain bound to GDP unlocks a cascade of large-domain movements in IF2 that propagate to the distal tRNA-binding domain C2. The C2-domain relocates 35 angstroms away from tRNA, explaining how IF2 makes way for fMet-tRNAi(fMet) accommodation into the P site. Our findings provide the basis by which IF2 gates the ribosome to the elongation phase.
 
Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation.,Basu RS, Sherman MB, Gagnon MG Nat Commun. 2022 Jun 13;13(1):3388. doi: 10.1038/s41467-022-31129-2. PMID:35697706<ref>PMID:35697706</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7uiu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Basu, R S]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Gagnon, M G]]
[[Category: Basu RS]]
[[Category: Sherman, M B]]
[[Category: Gagnon MG]]
[[Category: 70s ribosome]]
[[Category: Sherman MB]]
[[Category: Conformational change]]
[[Category: Cryo-em]]
[[Category: Initiation factor 2]]
[[Category: Initiator trna]]
[[Category: Ribosome]]
[[Category: Translation initiation]]
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