2d3n: Difference between revisions
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==Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose== | ==Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose== | ||
<StructureSection load='2d3n' size='340' side='right' caption='[[2d3n]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2d3n' size='340' side='right' caption='[[2d3n]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wp6|1wp6]], [[1wpc|1wpc]], [[2d3l|2d3l]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wp6|1wp6]], [[1wpc|1wpc]], [[2d3l|2d3l]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltohexaosidase Glucan 1,4-alpha-maltohexaosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.98 3.2.1.98] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltohexaosidase Glucan 1,4-alpha-maltohexaosidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3n OCA], [http://pdbe.org/2d3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d3n RCSB], [http://www.ebi.ac.uk/pdbsum/2d3n PDBsum]</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=2d3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3n OCA], [http://pdbe.org/2d3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d3n RCSB], [http://www.ebi.ac.uk/pdbsum/2d3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/2d3n_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/2d3n_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Amylase|Amylase]] | *[[Amylase|Amylase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:22, 30 May 2018
Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaoseCrystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose
Structural highlights
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 PubMedMaltohexaose-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 AlsoReferences
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