5hh1: Difference between revisions

(3 intermediate revisions by the same user not shown)

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5hh1 is ~~ON HOLD until Paper~~ Publication

==Crystal structure of human Naa60 mutant - F34A in complex with CoA==

== Structural highlights ==

<table><tr><td colspan='2'>[[5hh1]] 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=5HH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HH1 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]] 1.803Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=5hh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hh1 OCA], [https://pdbe.org/5hh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hh1 RCSB], [https://www.ebi.ac.uk/pdbsum/5hh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hh1 ProSAT]</span></td></tr>

</table>

== 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>

== 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.

~~Authors: Chen~~, ~~J.Y~~., Liu, L., Yun~~, C~~.H.

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Liu, L~~]]

[[Category: ~~Yun, C.H~~]]

== References ==

[[Category: ~~Chen, J.Y~~]]

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Chen JY]]

[[Category: Liu L]]

[[Category: Yun CH]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5hh1 is ON HOLD  until Paper Publication
+==Crystal structure of human Naa60 mutant - F34A in complex with CoA==
+<StructureSection load='5hh1' size='340' side='right'caption='[[5hh1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5hh1]] 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=5HH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HH1 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]] 1.803&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=5hh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hh1 OCA], [https://pdbe.org/5hh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hh1 RCSB], [https://www.ebi.ac.uk/pdbsum/5hh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hh1 ProSAT]</span></td></tr>
+</table>
+== 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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Chen, J.Y., Liu, L., Yun, C.H.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Liu, L]]
+<div class="pdbe-citations 5hh1" style="background-color:#fffaf0;"></div>
-[[Category: Yun, C.H]]
+== References ==
-[[Category: Chen, J.Y]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chen JY]]
+[[Category: Liu L]]
+[[Category: Yun CH]]