1J10

beta-amylase from Bacillus cereus var. mycoides in complex with GGX

Summary for 1J10

• Entry DOI: 10.2210/pdb1j10/pdb
• Related: 1J0Y 1J0Z 1J11 1J12 5BCA
• Descriptor: Beta-amylase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-xylopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-xylopyranose, ... (5 entities in total)
• Functional Keywords: hydrolase, beta-amylase, raw-starch binding domain
• Biological source: Bacillus cereus
• Total number of polymer chains: 4
• Total formula weight: 237389.70

Authors

Oyama, T.,Miyake, H.,Kusunoki, M.,Nitta, Y. (deposition date: 2002-11-25, release date: 2003-06-17, Last modification date: 2024-11-13)

Primary citation

Oyama, T.,Miyake, H.,Kusunoki, M.,Nitta, Y.
Crystal Structures of beta-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents
J.BIOCHEM.(TOKYO), 133:467-474, 2003

PubMed Abstract: 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-xylopyranose (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.

PubMed: 12761294
DOI: 10.1093/jb/mvg061

Experimental method

X-RAY DIFFRACTION (2.1 Å)