5ot1
From Proteopedia
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<StructureSection load='5ot1' size='340' side='right' caption='[[5ot1]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5ot1' size='340' side='right' caption='[[5ot1]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5ot1]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OT1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ot1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermococcus_kodakaraensis"_atomi_et_al._2004 "thermococcus kodakaraensis" atomi et al. 2004]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OT1 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK0977 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 "Thermococcus kodakaraensis" Atomi et al. 2004])</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=5ot1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ot1 OCA], [http://pdbe.org/5ot1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ot1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ot1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ot1 ProSAT]</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=5ot1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ot1 OCA], [http://pdbe.org/5ot1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ot1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ot1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ot1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Thermococcus kodakaraensis atomi et al. 2004]] | ||
[[Category: Ahmad, N]] | [[Category: Ahmad, N]] | ||
[[Category: Akhtar, M]] | [[Category: Akhtar, M]] | ||
Revision as of 05:52, 25 April 2018
The type III pullulan hydrolase from Thermococcus kodakarensis
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