View source for 6yzz


==Arabidopsis thaliana Naa50 in complex with AcCoA==
<StructureSection load='6yzz' size='340' side='right'caption='[[6yzz]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yzz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YZZ 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]] 1.79&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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=6yzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yzz OCA], [https://pdbe.org/6yzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yzz RCSB], [https://www.ebi.ac.uk/pdbsum/6yzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yzz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9LFM3_ARATH Q9LFM3_ARATH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The majority of eukaryotic proteins is modified by N-terminal acetylation, which plays a fundamental role in protein homeostasis, localization, and complex formation. N-terminal acetyltransferases (NATs) mainly act co-translationally on newly synthesized proteins at the ribosomal tunnel exit. NatA is the major NAT consisting of Naa10 catalytic and Naa15 auxiliary subunits, and with Naa50 forms the NatE complex. Naa50 has recently been identified in Arabidopsis thaliana and is important for plant development and stress response regulation. Here, we determined high-resolution X-ray crystal structures of AtNaa50 in complex with AcCoA and a bisubstrate analog. We characterized its substrate specificity, determined its enzymatic parameters, and identified functionally important residues. Even though Naa50 is conserved among species, we highlight differences between Arabidopsis and yeast, where Naa50 is catalytically inactive but binds CoA conjugates. Our study provides insights into Naa50 conservation, species-specific adaptations, and serves as a basis for further studies of NATs in plants.

Structural and functional characterization of the N-terminal acetyltransferase Naa50.,Weidenhausen J, Kopp J, Armbruster L, Wirtz M, Lapouge K, Sinning I Structure. 2020 Dec 22. pii: S0969-2126(20)30471-8. doi:, 10.1016/j.str.2020.12.004. PMID:33400917<ref>PMID:33400917</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yzz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Kopp J]]
[[Category: Lapouge K]]
[[Category: Sinning I]]
[[Category: Weidenhausen J]]