5c88
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form== |
| + | <StructureSection load='5c88' size='340' side='right' caption='[[5c88]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5c88]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C88 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_alpha-N-acetyltransferase Peptide alpha-N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.88 2.3.1.88] </span></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=5c88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c88 OCA], [http://pdbe.org/5c88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c88 RCSB], [http://www.ebi.ac.uk/pdbsum/5c88 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5c88" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Chang, Y | + | <references/> |
| - | [[Category: Hsu, C | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Peptide alpha-N-acetyltransferase]] | ||
| + | [[Category: Chang, Y Y]] | ||
| + | [[Category: Hsu, C H]] | ||
| + | [[Category: Acetyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 20:13, 13 January 2016
Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form
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