5c88: Difference between revisions

Line 1:

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

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

== 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>

== 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.

~~The entry 5c88 is ON HOLD until Paper Publication~~

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>

~~Authors: Chang~~, Y.Y.~~, Hsu, C.H~~.

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

</div>

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

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

== References ==

[[Category: Chang, Y.Y]]

[[Category: Hsu, C.H]]

__TOC__

</StructureSection>

[[Category: Peptide alpha-N-acetyltransferase]]

[[Category: Chang, Y Y]]

[[Category: Hsu, C H]]

[[Category: Acetyltransferase]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form==
+<StructureSection load='5c88' size='340' side='right' caption='[[5c88]], [[Resolution|resolution]] 2.49&Aring;' 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.
-The entry 5c88 is ON HOLD  until Paper Publication
+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>
-Authors: Chang, Y.Y., Hsu, C.H.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form
+<div class="pdbe-citations 5c88" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Chang, Y.Y]]
+<references/>
-[[Category: Hsu, C.H]]
+__TOC__
+</StructureSection>
+[[Category: Peptide alpha-N-acetyltransferase]]
+[[Category: Chang, Y Y]]
+[[Category: Hsu, C H]]
+[[Category: Acetyltransferase]]
+[[Category: Transferase]]