2d3l: Difference between revisions
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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/ | <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=' | </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=' | <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> | ||
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<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: | [[Category: Bacillus sp. 707]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Akiba | [[Category: Akiba T]] | ||
[[Category: Haga | [[Category: Haga K]] | ||
[[Category: Harata | [[Category: Harata K]] | ||
[[Category: Kanai | [[Category: Kanai R]] | ||
[[Category: Yamane | [[Category: Yamane K]] | ||
Latest revision as of 11:23, 25 October 2023
Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose.Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose.
Structural highlights
FunctionEvolutionary 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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