View source for 5ot1


==The type III pullulan hydrolase from Thermococcus kodakarensis==
<StructureSection load='5ot1' size='340' side='right'caption='[[5ot1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ot1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OT1 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5ot1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ot1 OCA], [https://pdbe.org/5ot1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ot1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ot1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ot1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5JID9_THEKO Q5JID9_THEKO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pullulan-hydrolysing enzymes, more commonly known as debranching enzymes for starch and other polysaccharides, are of great interest and have been widely used in the starch-saccharification industry. Type III pullulan hydrolase from Thermococcus kodakarensis (TK-PUL) possesses both pullulanase and alpha-amylase activities. Until now, only two enzymes in this class, which are capable of hydrolysing both alpha-1,4- and alpha-1,6-glycosidic bonds in pullulan to produce a mixture of maltose, panose and maltotriose, have been described. TK-PUL shows highest activity in the temperature range 95-100 degrees C and has a pH optimum in the range 3.5-4.2. Its unique ability to hydrolyse maltotriose into maltose and glucose has not been reported for other homologous enzymes. The crystal structure of TK-PUL has been determined at a resolution of 2.8 A and represents the first analysis of a type III pullulan hydrolyse. The structure reveals that the last part of the N-terminal domain and the C-terminal domain are significantly different from homologous structures. In addition, the loop regions at the active-site end of the central catalytic domain are quite different. The enzyme has a well defined calcium-binding site and possesses a rare vicinal disulfide bridge. The thermostability of TK-PUL and its homologues may be attributable to several factors, including the increased content of salt bridges, helical segments, Pro, Arg and Tyr residues and the decreased content of serine.

Structure and function of the type III pullulan hydrolase from Thermococcus kodakarensis.,Guo J, Coker AR, Wood SP, Cooper JB, Keegan RM, Ahmad N, Muhammad MA, Rashid N, Akhtar M Acta Crystallogr D Struct Biol. 2018 Apr 1;74(Pt 4):305-314. doi:, 10.1107/S2059798318001754. Epub 2018 Apr 3. PMID:29652257<ref>PMID:29652257</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ot1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus kodakarensis]]
[[Category: Ahmad N]]
[[Category: Akhtar M]]
[[Category: Coker AR]]
[[Category: Cooper JB]]
[[Category: Guo J]]
[[Category: Keegan R]]
[[Category: Muhammad MA]]
[[Category: Rashid N]]
[[Category: Wood SP]]