View source for 4ua3


==Crystal structure of selenomethionine labeled SpNatD==
<StructureSection load='4ua3' size='340' side='right'caption='[[4ua3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ua3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UA3 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</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=4ua3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ua3 OCA], [https://pdbe.org/4ua3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ua3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ua3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ua3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAA40_SCHPO NAA40_SCHPO] N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A.[UniProtKB:Q04751][UniProtKB:Q86UY6]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-terminal acetylation is among the most common protein modifications in eukaryotes and is mediated by evolutionarily conserved N-terminal acetyltransferases (NATs). NatD is among the most selective NATs; its only known substrates are histones H4 and H2A, containing the N-terminal sequence SGRGK in humans. Here we characterize the molecular basis for substrate-specific acetylation by NatD by reporting its crystal structure bound to cognate substrates and performing related biochemical studies. A novel N-terminal segment wraps around the catalytic core domain to make stabilizing interactions, and the alpha1-alpha2 and beta6-beta7 loops adopt novel conformations to properly orient the histone N termini in the binding site. Ser1 and Arg3 of the histone make extensive contacts to highly conserved NatD residues in the substrate binding pocket, and flanking glycine residues also appear to contribute to substrate-specific binding by NatD, together defining a Ser-Gly-Arg-Gly recognition sequence. These studies have implications for understanding substrate-specific acetylation by NAT enzymes.

The Molecular Basis for Histone H4- and H2A-Specific Amino-Terminal Acetylation by NatD.,Magin RS, Liszczak GP, Marmorstein R Structure. 2015 Feb 3;23(2):332-41. doi: 10.1016/j.str.2014.10.025. Epub 2015 Jan, 22. PMID:25619998<ref>PMID:25619998</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ua3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Liszczak GP]]
[[Category: Magin RS]]
[[Category: Marmorstein R]]