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| | ==Structure of Naa15/Naa10 bound to HypK-THB== | | ==Structure of Naa15/Naa10 bound to HypK-THB== |
| - | <StructureSection load='5nnr' size='340' side='right' caption='[[5nnr]], [[Resolution|resolution]] 3.10Å' scene=''> | + | <StructureSection load='5nnr' size='340' side='right'caption='[[5nnr]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nnr]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NNR FirstGlance]. <br> | + | <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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0031530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=209285 CBS 144.50]), CTHT_0063490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=209285 CBS 144.50]), CTHT_0058830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=209285 CBS 144.50])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nnr OCA], [http://pdbe.org/5nnr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nnr RCSB], [http://www.ebi.ac.uk/pdbsum/5nnr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nnr ProSAT]</span></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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0S4M4_CHATD G0S4M4_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 144 50]] | + | [[Category: Chaetomium thermophilum]] |
| - | [[Category: Gumiero, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Kopp, J]] | + | [[Category: Gumiero A]] |
| - | [[Category: Sinning, I]]
| + | [[Category: Kopp J]] |
| - | [[Category: Weyer, F A]]
| + | [[Category: Sinning I]] |
| - | [[Category: Ard1]] | + | [[Category: Weyer FA]] |
| - | [[Category: Hypk]] | + | |
| - | [[Category: N-acetylation]] | + | |
| - | [[Category: Naa10]]
| + | |
| - | [[Category: Naa15]]
| + | |
| - | [[Category: Nat1]]
| + | |
| - | [[Category: Nata]]
| + | |
| - | [[Category: Nat]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
G0S4M4_CHATD
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I. Structural basis of HypK regulating N-terminal acetylation by the NatA complex. Nat Commun. 2017 Jun 6;8:15726. doi: 10.1038/ncomms15726. PMID:28585574 doi:http://dx.doi.org/10.1038/ncomms15726
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