6m6t: Difference between revisions
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==Amylomaltase from Streptococcus agalactiae in complex with acarbose== | ==Amylomaltase from Streptococcus agalactiae in complex with acarbose== | ||
<StructureSection load='6m6t' size='340' side='right'caption='[[6m6t]]' scene=''> | <StructureSection load='6m6t' size='340' side='right'caption='[[6m6t]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M6T FirstGlance]. <br> | <table><tr><td colspan='2'>[[6m6t]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M6T FirstGlance]. <br> | ||
</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=6m6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m6t OCA], [https://pdbe.org/6m6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m6t RCSB], [https://www.ebi.ac.uk/pdbsum/6m6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m6t ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=ASO:1,5-ANHYDROSORBITOL'>ASO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900007:alpha-acarbose'>PRD_900007</scene>, <scene name='pdbligand=PRD_900110:acarbose-derived+trisaccharide'>PRD_900110</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=6m6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m6t OCA], [https://pdbe.org/6m6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m6t RCSB], [https://www.ebi.ac.uk/pdbsum/6m6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m6t ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0E1EIJ0_STRAG A0A0E1EIJ0_STRAG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Amylomaltase (AM) catalyzes transglycosylation of starch to form linear or cyclic oligosaccharides with potential applications in biotechnology and industry. In the present work, a novel AM from the mesophilic bacterium Streptococcus agalactiae (SaAM), with 18-49% sequence identity to previously reported AMs, was characterized. Cyclization and disproportionation activities were observed with the optimum temperature of 30 degrees C and 40 degrees C, respectively. Structural determination of SaAM, the first crystal structure of small AMs from the mesophiles, revealed a glycosyl-enzyme intermediate derived from acarbose and a second acarbose molecule attacking the intermediate. This pre-transglycosylation conformation has never been before observed in AMs. Structural analysis suggests that thermostability in AMs might be mainly caused by an increase in salt bridges since SaAM has a lower number of salt bridges compared with AMs from the thermophiles. Increase in thermostability by mutation was performed. C446 was substituted with A/S/P. C446A showed higher activities and higher kcat/Km values for starch in comparison to the WT enzyme. C446S exhibited a 5 degrees C increase in optimum temperature and the threefold increase in half-life time at 45 degrees C, most likely resulting from H-bonding interactions. For all enzymes, the main large-ring cyclodextrin (LR-CD) products were CD24-CD26 with CD22 as the smallest. C446S produced more CD35-CD42, especially at a longer incubation time. | |||
Streptococcus agalactiae amylomaltase offers insight into the transglycosylation mechanism and the molecular basis of thermostability among amylomaltases.,Tumhom S, Nimpiboon P, Wangkanont K, Pongsawasdi P Sci Rep. 2021 Mar 24;11(1):6740. doi: 10.1038/s41598-021-85769-3. PMID:33762620<ref>PMID:33762620</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6m6t" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Streptococcus agalactiae]] | |||
[[Category: Pongsawasdi P]] | [[Category: Pongsawasdi P]] | ||
[[Category: Tumhom S]] | [[Category: Tumhom S]] | ||
[[Category: Wangkanont K]] | [[Category: Wangkanont K]] | ||
Latest revision as of 15:19, 29 November 2023
Amylomaltase from Streptococcus agalactiae in complex with acarbose
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