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4b9y
From Proteopedia
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| - | [[Image:4b9y.png|left|200px]] | ||
| - | + | ==Crystal Structure of Apo Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31== | |
| + | <StructureSection load='4b9y' size='340' side='right'caption='[[4b9y]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4b9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b9z|4b9z]], [[4ba0|4ba0]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></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=4b9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9y OCA], [https://pdbe.org/4b9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b9y RCSB], [https://www.ebi.ac.uk/pdbsum/4b9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/OL4AG_CELJU OL4AG_CELJU]] Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.<ref>PMID:23132856</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The metabolism of the storage polysaccharides glycogen and starch are of vital importance to organisms from all domains of life. In bacteria, utilization of these alpha-glucans requires the concerted action of a variety of enzymes, including glycoside hydrolases, glycoside phosphorylases, and transglycosylases. In particular, transglycosylases from glycoside hydrolase families GH13 and GH77 play well-established roles in alpha-glucan sidechain (de)branching, regulation of oligo- and polysaccharide chain length, and formation of cyclic dextrans. Here, we present the biochemical and tertiary structural characterization of a new type of bacterial 1,4-alpha-glucan 4-alpha-glucosyltransferase from glycoside hydrolase family 31 (GH31). Distinct from 1,4-alpha-glucan 6-alpha-glucosyltransferases (EC 2.4.1.24) and 4-alpha-glucanotransferases (EC 2.4.1.25), this enzyme strictly transferred one glucosyl residue from alpha(1 -->4) glucans in disproportionation reactions. Substrate hydrolysis was undetectable for a series of malto-oligosaccharides, except maltose, for which transglycosylation nonetheless dominated across a range of substrate concentrations. Crystallographic analysis of the enzyme in apo, acarbose-complexed, and trapped 5-beta-fluoroglucosyl-enzyme intermediate forms revealed extended substrate interactions across one negative and up to three positive subsites, thus providing structural rationalization for the unique, single-monosaccharide transferase activity of the enzyme. | ||
| - | + | Structural enzymology of Cellvibrio japonicus Agd31B reveals alpha-transglucosylase activity in glycoside hydrolase family 31.,Larsbrink J, Izumi A, Hemsworth GR, Davies GJ, Brumer H J Biol Chem. 2012 Nov 6. PMID:23132856<ref>PMID:23132856</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 4b9y" style="background-color:#fffaf0;"></div> |
| - | [[ | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cellvibrio cellulosa nagy et al. 2002]] | ||
[[Category: Alpha-glucosidase]] | [[Category: Alpha-glucosidase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Brumer, H | + | [[Category: Brumer, H]] |
| - | [[Category: Davies, G J | + | [[Category: Davies, G J]] |
| - | [[Category: Hemsworth, G R | + | [[Category: Hemsworth, G R]] |
| - | [[Category: Izumi, A | + | [[Category: Izumi, A]] |
| - | [[Category: Larsbrink, J | + | [[Category: Larsbrink, J]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Current revision
Crystal Structure of Apo Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31
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