1wp6
From Proteopedia
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|PDB= 1wp6 |SIZE=350|CAPTION= <scene name='initialview01'>1wp6</scene>, resolution 2.1Å | |PDB= 1wp6 |SIZE=350|CAPTION= <scene name='initialview01'>1wp6</scene>, resolution 2.1Å | ||
|SITE= | |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> | + | |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>, <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] | + | |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= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wp6 OCA], [http://www.ebi.ac.uk/pdbsum/1wp6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wp6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kanai, R.]] | [[Category: Kanai, R.]] | ||
[[Category: Yamane, K.]] | [[Category: Yamane, K.]] | ||
- | [[Category: CA]] | ||
- | [[Category: NA]] | ||
- | [[Category: PO4]] | ||
- | [[Category: TRS]] | ||
[[Category: alpha-amylase]] | [[Category: alpha-amylase]] | ||
[[Category: maltohexaose]] | [[Category: maltohexaose]] | ||
- | ''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 00:39:16 2008'' |
Revision as of 21:39, 30 March 2008
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, resolution 2.1Å | |||||||
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Ligands: | , , , | ||||||
Activity: | Glucan 1,4-alpha-maltohexaosidase, with EC number 3.2.1.98 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.
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
1WP6 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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