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| | <StructureSection load='2d3l' size='340' side='right'caption='[[2d3l]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2d3l' size='340' side='right'caption='[[2d3l]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2d3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacs7 Bacs7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2d3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._707 Bacillus sp. 707]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3L FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wp6|1wp6]], [[1wpc|1wpc]], [[2d3n|2d3n]]</div></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>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900030:alpha-maltopentaose'>PRD_900030</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltohexaosidase Glucan 1,4-alpha-maltohexaosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.98 3.2.1.98] </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=2d3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3l OCA], [https://pdbe.org/2d3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3l RCSB], [https://www.ebi.ac.uk/pdbsum/2d3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3l ProSAT]</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=2d3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3l OCA], [https://pdbe.org/2d3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d3l RCSB], [https://www.ebi.ac.uk/pdbsum/2d3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AMT6_BACS7 AMT6_BACS7] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacs7]] | + | [[Category: Bacillus sp. 707]] |
| - | [[Category: Glucan 1,4-alpha-maltohexaosidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Akiba, T]] | + | [[Category: Akiba T]] |
| - | [[Category: Haga, K]] | + | [[Category: Haga K]] |
| - | [[Category: Harata, K]] | + | [[Category: Harata K]] |
| - | [[Category: Kanai, R]] | + | [[Category: Kanai R]] |
| - | [[Category: Yamane, K]] | + | [[Category: Yamane K]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ligand binding]]
| + | |
| - | [[Category: Protein-carbohydrate complex]]
| + | |
| Structural highlights
2d3l is a 1 chain structure with sequence from Bacillus sp. 707. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AMT6_BACS7
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Maltohexaose-producing amylase (G6-amylase) from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) in the yield of >30% of the total products from short-chain amylose (DP=17). Our previous crystallographic study showed that G6-amylase has nine subsites, from -6 to +3, and pointed out the importance of the indole moiety of Trp140 in G6 production. G6-amylase has very low levels of hydrolytic activities for oligosaccharides shorter than maltoheptaose. To elucidate the mechanism underlying G6 production, we determined the crystal structures of the G6-amylase complexes with G6 and maltopentaose (G5). In the active site of the G6-amylase/G5 complex, G5 is bound to subsites -6 to -2, while G1 and G6 are found at subsites +2 and -7 to -2, respectively, in the G6-amylase/G6 complex. In both structures, the glucosyl residue located at subsite -6 is stacked to the indole moiety of Trp140 within a distance of 4A. The measurement of the activities of the mutant enzymes when Trp140 was replaced by leucine (W140L) or by tyrosine (W140Y) showed that the G6 production from short-chain amylose by W140L is lower than that by W140Y or wild-type enzyme. The face-to-face short contact between Trp140 and substrate sugars is suggested to regulate the disposition of the glucosyl residue at subsite -6 and to govern product specificity for G6 production.
Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.,Kanai R, Haga K, Akiba T, Yamane K, Harata K Protein Sci. 2006 Mar;15(3):468-77. Epub 2006 Feb 1. PMID:16452622[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kanai R, Haga K, Akiba T, Yamane K, Harata K. Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707. Protein Sci. 2006 Mar;15(3):468-77. Epub 2006 Feb 1. PMID:16452622 doi:http://dx.doi.org/10.1110/ps.051877006
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