4lx9: Difference between revisions
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==Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A== | ==Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A== | ||
<StructureSection load='4lx9' size='340' side='right' caption='[[4lx9]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='4lx9' size='340' side='right'caption='[[4lx9]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lx9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4lx9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LX9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | </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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4lx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lx9 OCA], [https://pdbe.org/4lx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lx9 RCSB], [https://www.ebi.ac.uk/pdbsum/4lx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lx9 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NAT_SACS2 NAT_SACS2] Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).<ref>PMID:17511810</ref> <ref>PMID:23959863</ref> <ref>PMID:25728374</ref> | |||
<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: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharolobus solfataricus P2]] | ||
[[Category: | [[Category: Liszczak GP]] | ||
[[Category: | [[Category: Marmorstein R]] | ||
Revision as of 13:38, 21 December 2022
Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme AArchaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A
Structural highlights
FunctionNAT_SACS2 Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).[1] [2] [3] Publication Abstract from PubMedAmino-terminal acetylation is a ubiquitous modification in eukaryotes that is involved in a growing number of biological processes. There are six known eukaryotic amino-terminal acetyltransferases (NATs), which are differentiated from one another on the basis of substrate specificity. To date, two eukaryotic NATs, NatA and NatE, have been structurally characterized, of which NatA will acetylate the alpha-amino group of a number of nonmethionine amino-terminal residue substrates such as serine; NatE requires a substrate amino-terminal methionine residue for activity. Interestingly, these two NATs use different catalytic strategies to accomplish substrate-specific acetylation. In archaea, where this modification is less prevalent, only one NAT enzyme has been identified. Surprisingly, this enzyme is able to acetylate NatA and NatE substrates and is believed to represent an ancestral NAT variant from which the eukaryotic NAT machinery evolved. To gain insight into the evolution of NAT enzymes, we determined the X-ray crystal structure of an archaeal NAT from Sulfolobus solfataricus (ssNAT). Through the use of mutagenesis and kinetic analysis, we show that the active site of ssNAT represents a hybrid of the NatA and NatE active sites, and we highlight features of this protein that allow it to facilitate catalysis of distinct substrates through different catalytic strategies, which is a unique characteristic of this enzyme. Taken together, the structural and biochemical data presented here have implications for the evolution of eukaryotic NAT enzymes and the substrate specificities therein. Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.,Liszczak G, Marmorstein R Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):14652-7. doi:, 10.1073/pnas.1310365110. Epub 2013 Aug 19. PMID:23959863[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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