3izy: Difference between revisions

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<SX load='3izy' size='340' side='right' viewer='molstar' caption='[[3izy]], [[Resolution|resolution]] 10.80&Aring;' scene=''>
<SX load='3izy' size='340' side='right' viewer='molstar' caption='[[3izy]], [[Resolution|resolution]] 10.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3izy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IZY FirstGlance]. <br>
<table><tr><td colspan='2'>[[3izy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZY FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3izz|3izz]]</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]] 10.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3izy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izy OCA], [http://pdbe.org/3izy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3izy RCSB], [http://www.ebi.ac.uk/pdbsum/3izy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3izy 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=3izy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izy OCA], [https://pdbe.org/3izy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3izy RCSB], [https://www.ebi.ac.uk/pdbsum/3izy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3izy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/IF2M_BOVIN IF2M_BOVIN]] 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.  
[https://www.uniprot.org/uniprot/IF2M_BOVIN IF2M_BOVIN] 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mitochondria have their own translational machineries for the synthesis of thirteen polypeptide chains that are components of the complexes that participate in the process of oxidative phosphorylation (or ATP generation). Translation initiation in mammalian mitochondria requires two initiation factors, IF2(mt) and IF3(mt), instead of the three that are present in eubacteria. The mammalian IF2(mt) possesses a unique 37 amino acid insertion domain, which is known to be important for the formation of the translation initiation complex. We have obtained a three-dimensional cryoelectron microscopic map of the mammalian IF2(mt) in complex with initiator and the eubacterial ribosome. We find that the 37 amino acid insertion domain interacts with the same binding site on the ribosome that would be occupied by the eubacterial initiation factor IF1, which is absent in mitochondria. Our finding suggests that the insertion domain of IF2(mt) mimics the function of eubacterial IF1, by blocking the ribosomal aminoacyl-tRNA binding site (A site) at the initiation step.
 
Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1.,Yassin AS, Haque ME, Datta PP, Elmore K, Banavali NK, Spremulli LL, Agrawal RK Proc Natl Acad Sci U S A. 2011 Mar 8;108(10):3918-23. Epub 2011 Feb 22. PMID:21368145<ref>PMID:21368145</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3izy" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
== References ==
<references/>
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__TOC__
</SX>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Agrawal, R K]]
[[Category: Agrawal RK]]
[[Category: Banavali, N K]]
[[Category: Banavali NK]]
[[Category: Datta, P P]]
[[Category: Datta PP]]
[[Category: Elmore, K]]
[[Category: Elmore K]]
[[Category: Haque, E]]
[[Category: Haque E]]
[[Category: Spremulli, L L]]
[[Category: Spremulli LL]]
[[Category: Yassin, A S]]
[[Category: Yassin AS]]
[[Category: E coli]]
[[Category: If2]]
[[Category: Ribosomal protein]]
[[Category: Rna]]
[[Category: Translation initiation factor 2]]

Latest revision as of 13:08, 21 February 2024

Mammalian mitochondrial translation initiation factor 2Mammalian mitochondrial translation initiation factor 2

3izy, resolution 10.80Å

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