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1j12
From Proteopedia
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[[Image:1j12.gif|left|200px]] | [[Image:1j12.gif|left|200px]] | ||
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'''Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG''' | '''Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG''' | ||
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[[Category: Nitta, Y.]] | [[Category: Nitta, Y.]] | ||
[[Category: Oyama, T.]] | [[Category: Oyama, T.]] | ||
| - | [[Category: | + | [[Category: Beta-amylase]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Raw-starch binding domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:40:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:40, 2 May 2008
Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG
Overview
The crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with five inhibitors were solved. The inhibitors used were three substrate analogs, i.e. glucose, maltose (product), and a synthesized compound, O-alpha-D-glucopyranosyl-(1-->4)-O-alpha-D-glucopyranosyl-(1-->4)-D-xylopy ranose (GGX), and two affinity-labeling reagents with an epoxy alkyl group at the reducing end of glucose. For all inhibitors, one molecule was bound at the active site cleft and the non-reducing end glucose of the four inhibitors except GGX was located at subsite 1, accompanied by a large conformational change of the flexible loop (residues 93-97), which covered the bound inhibitor. In addition, another molecule of maltose or GGX was bound about 30 A away from the active site. A large movement of residues 330 and 331 around subsite 3 was also observed upon the binding of GGX at subsites 3 to 5. Two affinity-labeling reagents, alpha-EPG and alpha-EBG, were covalently bound to a catalytic residue (Glu-172). A substrate recognition mechanism for the beta-amylase was discussed based on the modes of binding of these inhibitors in the active site cleft.
About this Structure
1J12 is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents., Oyama T, Miyake H, Kusunoki M, Nitta Y, J Biochem. 2003 Apr;133(4):467-74. PMID:12761294 Page seeded by OCA on Fri May 2 20:40:22 2008
