1wp6: Difference between revisions
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[[Image:1wp6.jpg|left|200px]] | [[Image:1wp6.jpg|left|200px]] | ||
'''Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.''' | {{Structure | ||
|PDB= 1wp6 |SIZE=350|CAPTION= <scene name='initialview01'>1wp6</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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 alkalophilic Bacillus sp.707.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WP6 is a [ | 1WP6 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=1WP6 OCA]. | ||
==Reference== | ==Reference== | ||
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:// | 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: maltohexaose]] | [[Category: maltohexaose]] | ||
''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 14:59:53 2008'' | ||
Revision as of 15:59, 20 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 alkalophilic Bacillus sp.707.
OverviewOverview
Maltohexaose-producing amylase, called G6-amylase (EC 3.2.1.98), from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) from starch and related alpha-1,4-glucans. To elucidate the reaction mechanism of G6-amylase, the enzyme activities were evaluated and crystal structures were determined for the native enzyme and its complex with pseudo-maltononaose at 2.1 and 1.9 A resolutions, respectively. The optimal condition for starch-degrading reaction activity was found at 45 degrees C and pH 8.8, and the enzyme produced G6 in a yield of more than 30% of the total products from short-chain amylose (DP = 17). The crystal structures revealed that Asp236 is a nucleophilic catalyst and Glu266 is a proton donor/acceptor. Pseudo-maltononaose occupies subsites -6 to +3 and induces the conformational change of Glu266 and Asp333 to form a salt linkage with the N-glycosidic amino group and a hydrogen bond with secondary hydroxyl groups of the cyclitol residue bound to subsite -1, respectively. The indole moiety of Trp140 is stacked on the cyclitol and 4-amino-6-deoxyglucose residues located at subsites -6 and -5 within a 4 A distance. Such a face-to-face short contact may regulate the disposition of the glucosyl residue at subsite -6 and would govern the product specificity for G6 production.
About this StructureAbout this Structure
1WP6 is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
ReferenceReference
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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