1j11
From Proteopedia
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|PDB= 1j11 |SIZE=350|CAPTION= <scene name='initialview01'>1j11</scene>, resolution 2.0Å | |PDB= 1j11 |SIZE=350|CAPTION= <scene name='initialview01'>1j11</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=EPG:2-HYDROXYMETHYL-6-OXIRANYLMETHOXY-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>EPG</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPG:2-HYDROXYMETHYL-6-OXIRANYLMETHOXY-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>EPG</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[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] </span> | |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[5bca|5BCA]], [[1j0y|1J0Y]], [[1j0z|1J0Z]], [[1j10|1J10]], [[1j12|1J12]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j11 OCA], [http://www.ebi.ac.uk/pdbsum/1j11 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j11 RCSB]</span> | ||
}} | }} | ||
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[[Category: Nitta, Y.]] | [[Category: Nitta, Y.]] | ||
[[Category: Oyama, T.]] | [[Category: Oyama, T.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: EPG]] | ||
[[Category: beta-amylase]] | [[Category: beta-amylase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: raw-starch binding domain]] | [[Category: raw-starch binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:26 2008'' |
Revision as of 18:27, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Beta-amylase, with EC number 3.2.1.2 | ||||||
| Related: | 5BCA, 1J0Y, 1J0Z, 1J10, 1J12
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
beta-amylase from Bacillus cereus var. mycoides in complex with alpha-EPG
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
1J11 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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