|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5hgz' size='340' side='right'caption='[[5hgz]], [[Resolution|resolution]] 1.38Å' scene=''> | | <StructureSection load='5hgz' size='340' side='right'caption='[[5hgz]], [[Resolution|resolution]] 1.38Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hgz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HGZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HGZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hgz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HGZ FirstGlance]. <br> |
| - | </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=MLA:MALONIC+ACID'>MLA</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]] 1.383Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hh0|5hh0]], [[5hh1|5hh1]]</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=MLA:MALONIC+ACID'>MLA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NAA60, HAT4, NAT15, UNQ2771/PRO7155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5hgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hgz OCA], [https://pdbe.org/5hgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hgz RCSB], [https://www.ebi.ac.uk/pdbsum/5hgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hgz ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hgz OCA], [http://pdbe.org/5hgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hgz RCSB], [http://www.ebi.ac.uk/pdbsum/5hgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hgz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAA60_HUMAN NAA60_HUMAN]] Histone acetyltransferase localized in the Golgi apparatus that mediates acetylation of free histone H4, thereby facilitating nucleosome assembly. Has a preference for free histone H4 'Lys-20'(H4K20ac), 'Lys-79'(H4K79ac) and 'Lys-91' (H4K91ac). Also displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase.<ref>PMID:21750686</ref> <ref>PMID:21981917</ref> | + | [https://www.uniprot.org/uniprot/NAA60_HUMAN NAA60_HUMAN] Histone acetyltransferase localized in the Golgi apparatus that mediates acetylation of free histone H4, thereby facilitating nucleosome assembly. Has a preference for free histone H4 'Lys-20'(H4K20ac), 'Lys-79'(H4K79ac) and 'Lys-91' (H4K91ac). Also displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase.<ref>PMID:21750686</ref> <ref>PMID:21981917</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, J Y]] | + | [[Category: Chen JY]] |
| - | [[Category: Liu, L]] | + | [[Category: Liu L]] |
| - | [[Category: Yun, C H]] | + | [[Category: Yun CH]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: N-terminal acetylation]]
| + | |
| - | [[Category: Nat]]
| + | |
| - | [[Category: Protein modificaiton]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NAA60_HUMAN Histone acetyltransferase localized in the Golgi apparatus that mediates acetylation of free histone H4, thereby facilitating nucleosome assembly. Has a preference for free histone H4 'Lys-20'(H4K20ac), 'Lys-79'(H4K79ac) and 'Lys-91' (H4K91ac). Also displays alpha (N-terminal) acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase.[1] [2]
Publication Abstract from PubMed
N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains. Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes. This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine N(epsilon)-acetyltransferase (KAT) activity to catalyze the acetylation of lysine epsilon-amine. Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA). The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the beta7-beta8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures. Remarkably, we found that the side-chain of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involving enzyme, co-factor and substrates interactions. Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved beta3-beta4 long loop participates in the regulation of hNaa60 activity.
Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase.,Chen JY, Liu L, Cao CL, Li MJ, Tan K, Yang X, Yun CH Sci Rep. 2016 Aug 23;6:31425. doi: 10.1038/srep31425. PMID:27550639[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T. NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 2011 Jul;7(7):e1002169. doi: 10.1371/journal.pgen.1002169. Epub 2011 , Jul 7. PMID:21750686 doi:http://dx.doi.org/10.1371/journal.pgen.1002169
- ↑ Yang X, Yu W, Shi L, Sun L, Liang J, Yi X, Li Q, Zhang Y, Yang F, Han X, Zhang D, Yang J, Yao Z, Shang Y. HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 and facilitates chromatin assembly. Mol Cell. 2011 Oct 7;44(1):39-50. doi: 10.1016/j.molcel.2011.07.032. PMID:21981917 doi:http://dx.doi.org/10.1016/j.molcel.2011.07.032
- ↑ Chen JY, Liu L, Cao CL, Li MJ, Tan K, Yang X, Yun CH. Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase. Sci Rep. 2016 Aug 23;6:31425. doi: 10.1038/srep31425. PMID:27550639 doi:http://dx.doi.org/10.1038/srep31425
|
