7mx2: Difference between revisions
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==Cryo-EM structure of human ternary NatC complex with a Bisubstrate inhibitor== | |||
<StructureSection load='7mx2' size='340' side='right'caption='[[7mx2]], [[Resolution|resolution]] 3.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7mx2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MX2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.64Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMC:CARBOXYMETHYL+COENZYME+*A'>CMC</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=7mx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mx2 OCA], [https://pdbe.org/7mx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mx2 RCSB], [https://www.ebi.ac.uk/pdbsum/7mx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mx2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NAA38_HUMAN NAA38_HUMAN] Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues (PubMed:19398576, PubMed:37891180). N-terminal acetylation protects proteins from ubiquitination and degradation by the N-end rule pathway (PubMed:37891180).<ref>PMID:19398576</ref> <ref>PMID:37891180</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a large auxiliary subunit that facilitates catalysis and ribosome targeting for co-translational acetylation. NatC is one of the major NATs containing an NAA30 catalytic subunit, but uniquely contains two auxiliary subunits, large NAA35 and small NAA38. Here, we report the cryo-EM structures of human NatC (hNatC) complexes with and without NAA38, together with biochemical studies, to reveal that NAA38 increases the thermostability and broadens the substrate-specificity profile of NatC by ordering an N-terminal segment of NAA35 and reorienting an NAA30 N-terminal peptide binding loop for optimal catalysis, respectively. We also note important differences in engagement with a stabilizing inositol hexaphosphate molecule between human and yeast NatC. These studies provide new insights for the function and evolution of the NatC complex. | |||
Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase.,Deng S, Gardner SM, Gottlieb L, Pan B, Petersson EJ, Marmorstein R Structure. 2023 Feb 2;31(2):166-173.e4. doi: 10.1016/j.str.2022.12.008. Epub 2023 , Jan 12. PMID:36638802<ref>PMID:36638802</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7mx2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Deng S]] | |||
[[Category: Marmorstein R]] | |||
