6ag5: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ag5 is ON HOLD
+==Crystal structure of Ard1 N-terminal acetyltransferase E88H/H127E mutant from Sulfolobus solfataricus==
+<StructureSection load='6ag5' size='340' side='right'caption='[[6ag5]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ag5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AG5 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]] 2.32&#8491;</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=CA:CALCIUM+ION'>CA</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=6ag5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ag5 OCA], [https://pdbe.org/6ag5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ag5 RCSB], [https://www.ebi.ac.uk/pdbsum/6ag5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ag5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NAT_SACS2 NAT_SACS2] Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).<ref>PMID:17511810</ref> <ref>PMID:23959863</ref> <ref>PMID:25728374</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The common mechanism of N-acetyltransferases (NATs) is a water-mediated catalysis, which is not conducive to thermophilic acetyltransferases. The crystal structure of SsArd1 shows an ordered catalytic water molecule in a trap formed by the residues H88 and E127. Structure-guided mutagenesis, kinetic studies and MD simulation indicated that the turnover rates of H88A, E127A and H88A/E127A mutants were low, but that of the H88E/E127H mutant could be restored to the level of the wild type.
-Authors: Chang, Y.Y., Hsu, C.H.
+Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism.,Chang YY, Hagawa S, Hsu CH Chem Commun (Camb). 2020 Sep 10;56(72):10537-10540. doi: 10.1039/d0cc04305b. PMID:32780067<ref>PMID:32780067</ref>
-Description: Crystal structure of Ard1 N-terminal acetyltransferase E88H/H127E mutant from Sulfolobus solfataricus
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Chang, Y.Y]]
+<div class="pdbe-citations 6ag5" style="background-color:#fffaf0;"></div>
-[[Category: Hsu, C.H]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharolobus solfataricus P2]]
+[[Category: Chang YY]]
+[[Category: Hsu CH]]