2d3l

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{{STRUCTURE_2d3l| PDB=2d3l | SCENE= }}
{{STRUCTURE_2d3l| PDB=2d3l | SCENE= }}
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'''Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose.'''
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===Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose.===
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==Overview==
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Maltohexaose-producing amylase (G6-amylase) from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) in the yield of &gt;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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16452622}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16452622 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16452622}}
==About this Structure==
==About this Structure==
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==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://www.ncbi.nlm.nih.gov/pubmed/16452622 16452622]
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]
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Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707., Kanai R, Haga K, Akiba T, Yamane K, Harata K, Biochemistry. 2004 Nov 9;43(44):14047-56. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15518553 15518553]
[[Category: Bacillus sp.]]
[[Category: Bacillus sp.]]
[[Category: Glucan 1,4-alpha-maltohexaosidase]]
[[Category: Glucan 1,4-alpha-maltohexaosidase]]
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[[Category: Ligand binding]]
[[Category: Ligand binding]]
[[Category: Protein-carbohydrate complex]]
[[Category: Protein-carbohydrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:38:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:36:34 2008''

Revision as of 03:36, 29 July 2008

Image:2d3l.png

Template:STRUCTURE 2d3l

Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose.

Template:ABSTRACT PUBMED 16452622

About this Structure

2D3L is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

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:16452622

Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707., Kanai R, Haga K, Akiba T, Yamane K, Harata K, Biochemistry. 2004 Nov 9;43(44):14047-56. PMID:15518553

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