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| | ==D308A mutant of Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase complexed with isomaltooctaose== | | ==D308A mutant of Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase complexed with isomaltooctaose== |
| - | <StructureSection load='3wnn' size='340' side='right' caption='[[3wnn]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='3wnn' size='340' side='right'caption='[[3wnn]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wnn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_24 Atcc 24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WNN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WNN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wnn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WNN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wnk|3wnk]], [[3wnl|3wnl]], [[3wnm|3wnm]], [[3wno|3wno]], [[3wnp|3wnp]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cit ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1397 ATCC 24])</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=3wnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wnn OCA], [https://pdbe.org/3wnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wnn RCSB], [https://www.ebi.ac.uk/pdbsum/3wnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wnn ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cycloisomaltooligosaccharide_glucanotransferase Cycloisomaltooligosaccharide glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.248 2.4.1.248] </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=3wnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wnn OCA], [http://pdbe.org/3wnn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wnn RCSB], [http://www.ebi.ac.uk/pdbsum/3wnn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wnn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CTA1_BACCI CTA1_BACCI]] Produces cycloisomaltooligosaccharide from dextran containing 7, 8 or 9 glucose units. The enzyme is specific for (1->6)-alpha-D-glucans (dextrans) and, without activity toward (1->4)-alpha-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points.<ref>PMID:7515357</ref> | + | [https://www.uniprot.org/uniprot/CTA1_NIACI CTA1_NIACI] Produces cycloisomaltooligosaccharide from dextran containing 7, 8 or 9 glucose units. The enzyme is specific for (1->6)-alpha-D-glucans (dextrans) and, without activity toward (1->4)-alpha-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points.<ref>PMID:7515357</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 24]] | + | [[Category: Large Structures]] |
| - | [[Category: Cycloisomaltooligosaccharide glucanotransferase]] | + | [[Category: Niallia circulans]] |
| - | [[Category: Fujimoto, Z]] | + | [[Category: Fujimoto Z]] |
| - | [[Category: Funane, K]] | + | [[Category: Funane K]] |
| - | [[Category: Kim, Y M]] | + | [[Category: Kim YM]] |
| - | [[Category: Kimura, A]] | + | [[Category: Kimura A]] |
| - | [[Category: Kishine, N]] | + | [[Category: Kishine N]] |
| - | [[Category: Kitamura, S]] | + | [[Category: Kitamura S]] |
| - | [[Category: Kobayashi, M]] | + | [[Category: Kobayashi M]] |
| - | [[Category: Momma, M]] | + | [[Category: Momma M]] |
| - | [[Category: Suzuki, N]] | + | [[Category: Suzuki N]] |
| - | [[Category: Suzuki, R]] | + | [[Category: Suzuki R]] |
| - | [[Category: Suzuki, S]] | + | [[Category: Suzuki S]] |
| - | [[Category: 6-glucan]]
| + | |
| - | [[Category: Alpha-1]]
| + | |
| - | [[Category: Beta-jelly roll]]
| + | |
| - | [[Category: C2 type immunoglobulin fold]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Greek key]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
3wnn is a 2 chain structure with sequence from Niallia circulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.25Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CTA1_NIACI Produces cycloisomaltooligosaccharide from dextran containing 7, 8 or 9 glucose units. The enzyme is specific for (1->6)-alpha-D-glucans (dextrans) and, without activity toward (1->4)-alpha-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points.[1]
Publication Abstract from PubMed
Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase belongs to the glycoside hydrolase family 66 and catalyzes an intramolecular transglucosylation reaction that produces cycloisomaltooligosaccharides from dextran. The crystal structure of the core fragment from Ser-39 to Met-738 of B. circulans T-3040 cycloisomaltooligosaccharide glucanotransferase, devoid of its N-terminal signal peptide and C-terminal nonconserved regions, was determined. The structural model contained one catalytic (beta/alpha)8-barrel domain and three beta-domains. Domain N with an immunoglobulin-like beta-sandwich fold was attached to the N terminus; domain C with a Greek key beta-sandwich fold was located at the C terminus, and a carbohydrate-binding module family 35 (CBM35) beta-jellyroll domain B was inserted between the 7th beta-strand and the 7th alpha-helix of the catalytic domain A. The structures of the inactive catalytic nucleophile mutant enzyme complexed with isomaltohexaose, isomaltoheptaose, isomaltooctaose, and cycloisomaltooctaose revealed that the ligands bound in the catalytic cleft and the sugar-binding site of CBM35. Of these, isomaltooctaose bound in the catalytic site extended to the second sugar-binding site of CBM35, which acted as subsite -8, representing the enzyme.substrate complex when the enzyme produces cycloisomaltooctaose. The isomaltoheptaose and cycloisomaltooctaose bound in the catalytic cleft with a circular structure around Met-310, representing the enzyme.product complex. These structures collectively indicated that CBM35 functions in determining the size of the product, causing the predominant production of cycloisomaltooctaose by the enzyme. The canonical sugar-binding site of CBM35 bound the mid-part of isomaltooligosaccharides, indicating that the original function involved substrate binding required for efficient catalysis.
Structural elucidation of the cyclization mechanism of alpha-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase.,Suzuki N, Fujimoto Z, Kim YM, Momma M, Kishine N, Suzuki R, Suzuki S, Kitamura S, Kobayashi M, Kimura A, Funane K J Biol Chem. 2014 Apr 25;289(17):12040-51. doi: 10.1074/jbc.M114.547992. Epub, 2014 Mar 10. PMID:24616103[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oguma T, Tobe K, Kobayashi M. Purification and properties of a novel enzyme from Bacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosaccharides. FEBS Lett. 1994 May 30;345(2-3):135-8. PMID:7515357
- ↑ Suzuki N, Fujimoto Z, Kim YM, Momma M, Kishine N, Suzuki R, Suzuki S, Kitamura S, Kobayashi M, Kimura A, Funane K. Structural elucidation of the cyclization mechanism of alpha-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase. J Biol Chem. 2014 Apr 25;289(17):12040-51. doi: 10.1074/jbc.M114.547992. Epub, 2014 Mar 10. PMID:24616103 doi:http://dx.doi.org/10.1074/jbc.M114.547992
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