2d3n: Difference between revisions
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[[Image:2d3n.gif|left|200px]] | [[Image:2d3n.gif|left|200px]] | ||
'''Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose''' | {{Structure | ||
|PDB= 2d3n |SIZE=350|CAPTION= <scene name='initialview01'>2d3n</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2D3N is a [ | 2D3N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3N OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16452622 16452622] | ||
[[Category: Bacillus sp.]] | [[Category: Bacillus sp.]] | ||
[[Category: Glucan 1,4-alpha-maltohexaosidase]] | [[Category: Glucan 1,4-alpha-maltohexaosidase]] | ||
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[[Category: protein-carbohydrate complex]] | [[Category: protein-carbohydrate complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:55 2008'' |
Revision as of 17:22, 20 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | , and | ||||||
Activity: | Glucan 1,4-alpha-maltohexaosidase, with EC number 3.2.1.98 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose
OverviewOverview
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.
About this StructureAbout this Structure
2D3N is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
ReferenceReference
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
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