5nnp: Difference between revisions
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==Structure of Naa15/Naa10 bound to HypK-THB== | |||
<StructureSection load='5nnp' size='340' side='right'caption='[[5nnp]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nnp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NNP 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]] 2.602Å</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>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5nnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nnp OCA], [https://pdbe.org/5nnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nnp RCSB], [https://www.ebi.ac.uk/pdbsum/5nnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nnp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G0S4M4_CHATD G0S4M4_CHATD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In eukaryotes, N-terminal acetylation is one of the most common protein modifications involved in a wide range of biological processes. Most N-acetyltransferase complexes (NATs) act co-translationally, with the heterodimeric NatA complex modifying the majority of substrate proteins. Here we show that the Huntingtin yeast two-hybrid protein K (HypK) binds tightly to the NatA complex comprising the auxiliary subunit Naa15 and the catalytic subunit Naa10. The crystal structures of NatA bound to HypK or to a N-terminal deletion variant of HypK were determined without or with a bi-substrate analogue, respectively. The HypK C-terminal region is responsible for high-affinity interaction with the C-terminal part of Naa15. In combination with acetylation assays, the HypK N-terminal region is identified as a negative regulator of the NatA acetylation activity. Our study provides mechanistic insights into the regulation of this pivotal protein modification. | |||
Structural basis of HypK regulating N-terminal acetylation by the NatA complex.,Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I Nat Commun. 2017 Jun 6;8:15726. doi: 10.1038/ncomms15726. PMID:28585574<ref>PMID:28585574</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Gumiero | <div class="pdbe-citations 5nnp" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Sinning | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Gumiero A]] | |||
[[Category: Kopp J]] | |||
[[Category: Sinning I]] | |||
[[Category: Weyer FA]] | |||
