1wpc
From Proteopedia
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| - | [[Image:1wpc.jpg|left|200px]] | + | [[Image:1wpc.jpg|left|200px]] |
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| - | '''Crystal structure of maltohexaose-producing amylase complexed with pseudo-maltononaose''' | + | {{Structure |
| + | |PDB= 1wpc |SIZE=350|CAPTION= <scene name='initialview01'>1wpc</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <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 complexed with pseudo-maltononaose''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WPC is a [ | + | 1WPC 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=1WPC 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-producing amylase]] | [[Category: maltohexaose-producing amylase]] | ||
| - | ''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 14:59:58 2008'' |
Revision as of 12:59, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 complexed with pseudo-maltononaose
Overview
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 Structure
1WPC is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
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:15518553
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