5hgz
From Proteopedia
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== Function == | == Function == | ||
[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> | [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> | ||
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| - | == 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. | ||
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| - | 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<ref>PMID:27550639</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 5hgz" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of human Naa60 in complex with acetyl-CoA
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Categories: Homo sapiens | Large Structures | Chen JY | Liu L | Yun CH
