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6tgx

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Current revision (07:38, 1 May 2024) (edit) (undo)
 
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<StructureSection load='6tgx' size='340' side='right'caption='[[6tgx]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='6tgx' size='340' side='right'caption='[[6tgx]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6tgx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TGX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TGX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6tgx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] 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=6TGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TGX FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g16800, F5E19.140, F5E19_140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tgx OCA], [http://pdbe.org/6tgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tgx RCSB], [http://www.ebi.ac.uk/pdbsum/6tgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tgx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tgx OCA], [https://pdbe.org/6tgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tgx RCSB], [https://www.ebi.ac.uk/pdbsum/6tgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tgx ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q6NLS5_ARATH Q6NLS5_ARATH]
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In humans and plants, N-terminal acetylation plays a central role in protein homeostasis, affects 80 % of proteins in the cytoplasm and is catalyzed by five ribosome-associated N-acetyltransferases (NatA-E). Humans also possess a Golgi-associated NatF (HsNAA60) that is essential for Golgi integrity. Remarkably, NAA60 is absent in fungi and was not identified in plants. Here we identify and characterize the first plasma membrane-anchored post-translationally acting N-acetyltransferase AtNAA60 in the reference plant Arabidopsis thaliana by the combined application of reverse genetics, global proteomics, live-cell imaging, microscale thermophoresis, CD-spectroscopy, nano differential scanning fluorometry, intrinsic tryptophan fluorescence and X-ray crystallography. We demonstrate that AtNAA60 like HsNAA60 is membrane-localized in vivo by an alpha-helical membrane anchor at its C-terminus, but in contrast to HsNAA60, AtNAA60 localizes to the plasma membrane. The AtNAA60 crystal structure provides insights into substrate-binding, the broad substrate specificity and the catalytic mechanism probed by structure-based mutagenesis. Characterization of the NAA60 loss-of-function mutants (naa60-1 and naa60-2) uncovers a plasma membrane-localized substrate of AtNAA60 and the importance of NAA60 during high salt stress. Our findings provide evidence for the plant-specific evolution of a plasma membrane-anchored N-acetyltransferase that is vital for adaptation to stress.
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The Arabidopsis N(alpha) -acetyltransferase NAA60 locates to the plasma membrane and is vital for the high salt stress response.,Linster E, Layer D, Bienvenut WV, Dinh TV, Weyer FA, Leemhuis W, Brunje A, Hoffrichter M, Miklankova P, Kopp J, Lapouge K, Sindlinger J, Schwarzer D, Meinnel T, Finkemeier I, Giglione C, Hell R, Sinning I, Wirtz M New Phytol. 2020 Jun 16. doi: 10.1111/nph.16747. PMID:32548857<ref>PMID:32548857</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6tgx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kopp, J]]
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[[Category: Synthetic construct]]
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[[Category: Lapouge, K]]
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[[Category: Kopp J]]
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[[Category: Layer, D]]
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[[Category: Lapouge K]]
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[[Category: Sinning, I]]
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[[Category: Layer D]]
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[[Category: N-alpha-acetyltransferase naa60 natf nat]]
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[[Category: Sinning I]]
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[[Category: Plant protein]]
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Current revision

Crystal structure of Arabidopsis thaliana NAA60 in complex with a bisubstrate analogue

PDB ID 6tgx

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