This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1j12
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 24: | Line 33: | ||
[[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
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 11:57:33 2008
