View source for 6yga


==Crystal structure of the apo NatC complex==
<StructureSection load='6yga' size='340' side='right'caption='[[6yga]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yga]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YGA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.397&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6yga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yga OCA], [https://pdbe.org/6yga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yga RCSB], [https://www.ebi.ac.uk/pdbsum/6yga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yga ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAA30_YEAST NAA30_YEAST] Catalytic component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus GAG protein and possibly GRH1.<ref>PMID:11274203</ref> <ref>PMID:17261844</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The heterotrimeric NatC complex, comprising the catalytic Naa30 and the two auxiliary subunits Naa35 and Naa38, co-translationally acetylates the N-termini of numerous eukaryotic target proteins. Despite its unique subunit composition, its essential role for many aspects of cellular function and its suggested involvement in disease, structure and mechanism of NatC have remained unknown. Here, we present the crystal structure of the Saccharomyces cerevisiae NatC complex, which exhibits a strikingly different architecture compared to previously described N-terminal acetyltransferase (NAT) complexes. Cofactor and ligand-bound structures reveal how the first four amino acids of cognate substrates are recognized at the Naa30-Naa35 interface. A sequence-specific, ligand-induced conformational change in Naa30 enables efficient acetylation. Based on detailed structure-function studies, we suggest a catalytic mechanism and identify a ribosome-binding patch in an elongated tip region of NatC. Our study reveals how NAT machineries have divergently evolved to N-terminally acetylate specific subsets of target proteins.

Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.,Grunwald S, Hopf LVM, Bock-Bierbaum T, Lally CCM, Spahn CMT, Daumke O Nat Commun. 2020 Nov 2;11(1):5506. doi: 10.1038/s41467-020-19321-8. PMID:33139728<ref>PMID:33139728</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yga" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Bock-Bierbaum T]]
[[Category: Daumke O]]
[[Category: Grunwald S]]
[[Category: Hopf L]]
[[Category: Lally CC]]
[[Category: Spahn CMT]]