6ag5: Difference between revisions

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 <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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AG5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ag5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs2 Sacs2]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6AG5 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=CA:CALCIUM+ION'>CA</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=CA:CALCIUM+ION'>CA</scene></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=6ag5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ag5 OCA], [http://pdbe.org/6ag5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ag5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ag5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ag5 ProSAT]</span></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AsArd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SACS2])</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=6ag5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ag5 OCA], [http://pdbe.org/6ag5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ag5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ag5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ag5 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-Nalpha-acetyltransferases (Nats) possess a wide range of important biological functions. Their structures can vary according to the first two residues of their substrate. However, the mechanisms of substrate recognition and catalysis of Nats are elusive. Here, we present two structure of Sulfolobus solfataricus Ard1 (SsArd1), a member of the NatA family, at 2.13 and 1.84 A. Both structures contain coenzyme A, while the latter also contains a substrate-derived peptide. Sequential structure-based mutagenesis revealed that mutations of critical residues for CoA binding decreased the binding affinity of SsArd1 by 3 ~ 7-fold. Superimposition of SsArd1 (NatA) with human Naa50p (NatE) showed significant differences in key residues of enzymes near the first amino-acid position of the substrate peptide (Glu35 for SsArd1 and Val29 for Naa50p). Further enzyme activity assays revealed that the substrate specificity of SsArd1 could be altered from SSGTPT to MEEKVG by a range of Glu35 mutants. These studies provide not only a molecular elucidation of substrate recognition and specificity for the NatA family, but also insight into how members of the NAT family distinguish between amino acids at the substrate N-terminus from the ancient monomeric archaeal Ard1.
+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.
-Structural Basis for Substrate-specific Acetylation of Nalpha-acetyltransferase Ard1 from Sulfolobus solfataricus.,Chang YY, Hsu CH Sci Rep. 2015 Mar 2;5:8673. doi: 10.1038/srep08673. PMID:25728374<ref>PMID:25728374</ref>
+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>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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 </StructureSection>
 [[Category: Large Structures]]
+[[Category: Sacs2]]
 [[Category: Chang, Y Y]]
 [[Category: Hsu, C H]]
 [[Category: Acetyltransferase]]
 [[Category: Transferase]]