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5c88

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'''Unreleased structure'''
 
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The entry 5c88 is ON HOLD until Paper Publication
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==Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form==
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<StructureSection load='5c88' size='340' side='right'caption='[[5c88]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5c88]] is a 2 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=5C88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C88 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c88 OCA], [https://pdbe.org/5c88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c88 RCSB], [https://www.ebi.ac.uk/pdbsum/5c88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c88 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Structural comparison indicates the loop region between beta3 and beta4 of SsArd1 was more extended than corresponding region of mesophilic Nats and formed a plastically hydrogen bond network mainly via two Ser residues. Strikingly, two single-point mutants showed ~3 degrees C decrease in melting temperature, while two other variants showed a ~7 degrees C decrease in melting temperature, which correlated to the seriously reducing enzymatic activity. To our knowledge, this is the first discovery of a loop region capable of remarkably improving protein thermostability and to provide a novel possibility to engineer heat-resistant proteins.
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Authors: Chang, Y.Y., Hsu, C.H.
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Multiple conformations of the loop region confers heat-resistance of SsArd1, a thermophilic NatA.,Chang YY, Hsu CH Chembiochem. 2015 Nov 23. doi: 10.1002/cbic.201500568. PMID:26593285<ref>PMID:26593285</ref>
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Description: Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Chang, Y.Y]]
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<div class="pdbe-citations 5c88" style="background-color:#fffaf0;"></div>
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[[Category: Hsu, C.H]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharolobus solfataricus P2]]
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[[Category: Chang YY]]
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[[Category: Hsu CH]]

Current revision

Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form

PDB ID 5c88

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