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5hgz

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Revision as of 07:05, 20 May 2020

Crystal structure of human Naa60 in complex with acetyl-CoA

Structural highlights

5hgz is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	5hh0, 5hh1
Gene:	NAA60, HAT4, NAT15, UNQ2771/PRO7155 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hgz"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human Naa60 in complex with acetyl-CoA==
-<StructureSection load='5hgz' size='340' side='right' caption='[[5hgz]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
+<StructureSection load='5hgz' size='340' side='right'caption='[[5hgz]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hgz]] is a 1 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HGZ FirstGlance]. <br>
+<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>
-</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=MLA:MALONIC+ACID'>MLA</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hh0|5hh0]], [[5hh1|5hh1]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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'>[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>
 == Function ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Chen, J Y]]
 [[Category: Liu, L]]

5hgz

From Proteopedia

Revision as of 07:05, 20 May 2020

Crystal structure of human Naa60 in complex with acetyl-CoA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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