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'''BACILLUS CEREUS BETA-AMYLASE APO FORM''' | '''BACILLUS CEREUS BETA-AMYLASE APO FORM''' | ||
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[[Category: Shinke, R.]] | [[Category: Shinke, R.]] | ||
[[Category: Utsumi, S.]] | [[Category: Utsumi, S.]] | ||
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Revision as of 11:13, 2 May 2008
BACILLUS CEREUS BETA-AMYLASE APO FORM
OverviewOverview
The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.93 A, and beta =101.95 degrees. The structures of free and maltose-bound beta-amylases were determined by X-ray crystallography at 2.1 and 2.5 A with R-factors of 0.170 and 0.164, respectively. The final model of the maltose-bound form comprises 516 amino acid residues, four maltose molecules, 275 water molecules, one Ca2+, one acetate, and one sulfate ion. The enzyme consists of a core (beta/alpha)8-barrel domain (residues 5-434) and a C-terminal starch-binding domain (residues 435-613). Besides the active site in the core where two maltose molecules are bound in tandem, two novel maltose-binding sites were found in the core L4 region and in the C-terminal domain. The structure of the core domain is similar to that of soybean beta-amylase except for the L4 maltose-binding site, whereas the C-terminal domain has the same secondary structure as domain E of cyclodextrin glucosyltransferase. These two maltose-binding sites are 32-36 A apart from the active site. These results indicate that the ability of B. cereus beta-amylase to digest raw starch can be attributed to the additional two maltose-binding sites.
About this StructureAbout this Structure
1B90 is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose., Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S, Biochemistry. 1999 Jun 1;38(22):7050-61. PMID:10353816 Page seeded by OCA on Fri May 2 11:13:32 2008