4lx9: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4lx9|  PDB=4lx9  |  SCENE=  }}
===Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A===
{{ABSTRACT_PUBMED_23959863}}


==About this Structure==
==Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A==
[[4lx9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochroconis_lascauxensis Ochroconis lascauxensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LX9 OCA].  
<StructureSection load='4lx9' size='340' side='right'caption='[[4lx9]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 
== Structural highlights ==
==Reference==
<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>
<ref group="xtra">PMID:023959863</ref><references group="xtra"/><references/>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
[[Category: Ochroconis lascauxensis]]
<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>
[[Category: Liszczak, G P.]]
<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>
[[Category: Marmorstein, R.]]
</table>
[[Category: Amino-terminal acetyltransferase]]
== Function ==
[[Category: Gnat fold]]
[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>
[[Category: Transferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharolobus solfataricus P2]]
[[Category: Liszczak GP]]
[[Category: Marmorstein R]]

Latest revision as of 15:22, 1 March 2024

Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme AArchaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A

Structural highlights

4lx9 is a 1 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

References

  1. ↑ Mackay DT, Botting CH, Taylor GL, White MF. An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus. Mol Microbiol. 2007 Jun;64(6):1540-8. doi: 10.1111/j.1365-2958.2007.05752.x. Epub , 2007 May 18. PMID:17511810 doi:http://dx.doi.org/10.1111/j.1365-2958.2007.05752.x
  2. ↑ Liszczak G, Marmorstein R. Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog. 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 doi:http://dx.doi.org/10.1073/pnas.1310365110
  3. ↑ Chang YY, Hsu CH. Structural Basis for Substrate-specific Acetylation of Nalpha-acetyltransferase Ard1 from Sulfolobus solfataricus. Sci Rep. 2015 Mar 2;5:8673. doi: 10.1038/srep08673. PMID:25728374 doi:http://dx.doi.org/10.1038/srep08673

4lx9, resolution 1.98Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4lx9&oldid=4075154"