5nnr
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5nnr is ON HOLD until Paper Publication Authors: Weyer, F.A., Gumiero, A., Kopp, J., Sinning, I. Description: Structure of Naa15/Naa10 bound to Hyp...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Naa15/Naa10 bound to HypK-THB== | |
| + | <StructureSection load='5nnr' size='340' side='right'caption='[[5nnr]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5nnr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NNR 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]] 3.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5nnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nnr OCA], [https://pdbe.org/5nnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nnr RCSB], [https://www.ebi.ac.uk/pdbsum/5nnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nnr 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 5nnr" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Sinning | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Chaetomium thermophilum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gumiero A]] | ||
| + | [[Category: Kopp J]] | ||
| + | [[Category: Sinning I]] | ||
| + | [[Category: Weyer FA]] | ||
Current revision
Structure of Naa15/Naa10 bound to HypK-THB
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