2d3n: Difference between revisions
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|PDB= 2d3n |SIZE=350|CAPTION= <scene name='initialview01'>2d3n</scene>, resolution 1.90Å | |PDB= 2d3n |SIZE=350|CAPTION= <scene name='initialview01'>2d3n</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1wp6|1WP6]], [[1wpc|1WPC]], [[2d3l|2D3L]] | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2d3n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d3n RCSB]</span> | |||
}} | }} | ||
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[[Category: Kanai, R.]] | [[Category: Kanai, R.]] | ||
[[Category: Yamane, K.]] | [[Category: Yamane, K.]] | ||
[[Category: ligand binding]] | [[Category: ligand binding]] | ||
[[Category: maltohexaose]] | [[Category: maltohexaose]] | ||
[[Category: protein-carbohydrate complex]] | [[Category: protein-carbohydrate complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:52 2008'' | ||
Revision as of 02:29, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Glucan 1,4-alpha-maltohexaosidase, with EC number 3.2.1.98 | ||||||
| Related: | 1WP6, 1WPC, 2D3L
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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