1j12: Difference between revisions
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[[Image:1j12.gif|left|200px]] | [[Image:1j12.gif|left|200px]] | ||
'''Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG''' | {{Structure | ||
|PDB= 1j12 |SIZE=350|CAPTION= <scene name='initialview01'>1j12</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=EBG:2-HYDROXYMETHYL-6-(2-OXIRANYL-ETHOXY)-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>EBG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-amylase Beta-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.2 3.2.1.2] | |||
|GENE= | |||
}} | |||
'''Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1J12 is a [ | 1J12 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J12 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12761294 12761294] | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Beta-amylase]] | [[Category: Beta-amylase]] | ||
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[[Category: raw-starch binding domain]] | [[Category: raw-starch binding domain]] | ||
''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 11:57:33 2008'' | ||
Revision as of 09:57, 20 March 2008
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| 1j12, resolution 2.1Å | |||||||||||||
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| Ligands: | EBG and CA | ||||||||||||
| Activity: | Beta-amylase, with EC number 3.2.1.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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