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1b90
From Proteopedia
(New page: 200px<br /><applet load="1b90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b90, resolution 2.5Å" /> '''BACILLUS CEREUS BETA-...) |
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| - | [[Image:1b90.gif|left|200px]]<br /><applet load="1b90" size=" | + | [[Image:1b90.gif|left|200px]]<br /><applet load="1b90" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b90, resolution 2.5Å" /> | caption="1b90, resolution 2.5Å" /> | ||
'''BACILLUS CEREUS BETA-AMYLASE APO FORM'''<br /> | '''BACILLUS CEREUS BETA-AMYLASE APO FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystals of beta-amylase from Bacillus cereus belong to space group | + | The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.93 A, and beta =101.95 degrees. The structures of free and maltose-bound beta-amylases were determined by X-ray crystallography at 2.1 and 2.5 A with R-factors of 0.170 and 0.164, respectively. The final model of the maltose-bound form comprises 516 amino acid residues, four maltose molecules, 275 water molecules, one Ca2+, one acetate, and one sulfate ion. The enzyme consists of a core (beta/alpha)8-barrel domain (residues 5-434) and a C-terminal starch-binding domain (residues 435-613). Besides the active site in the core where two maltose molecules are bound in tandem, two novel maltose-binding sites were found in the core L4 region and in the C-terminal domain. The structure of the core domain is similar to that of soybean beta-amylase except for the L4 maltose-binding site, whereas the C-terminal domain has the same secondary structure as domain E of cyclodextrin glucosyltransferase. These two maltose-binding sites are 32-36 A apart from the active site. These results indicate that the ability of B. cereus beta-amylase to digest raw starch can be attributed to the additional two maltose-binding sites. |
==About this Structure== | ==About this Structure== | ||
| - | 1B90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with ACT, SO4 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1B90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B90 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:47 2008'' |
Revision as of 09:52, 21 February 2008
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BACILLUS CEREUS BETA-AMYLASE APO FORM
Overview
The crystals of beta-amylase from Bacillus cereus belong to space group P21 with the following cell dimensions: a = 57.70 A, b = 92.87 A, c = 65.93 A, and beta =101.95 degrees. The structures of free and maltose-bound beta-amylases were determined by X-ray crystallography at 2.1 and 2.5 A with R-factors of 0.170 and 0.164, respectively. The final model of the maltose-bound form comprises 516 amino acid residues, four maltose molecules, 275 water molecules, one Ca2+, one acetate, and one sulfate ion. The enzyme consists of a core (beta/alpha)8-barrel domain (residues 5-434) and a C-terminal starch-binding domain (residues 435-613). Besides the active site in the core where two maltose molecules are bound in tandem, two novel maltose-binding sites were found in the core L4 region and in the C-terminal domain. The structure of the core domain is similar to that of soybean beta-amylase except for the L4 maltose-binding site, whereas the C-terminal domain has the same secondary structure as domain E of cyclodextrin glucosyltransferase. These two maltose-binding sites are 32-36 A apart from the active site. These results indicate that the ability of B. cereus beta-amylase to digest raw starch can be attributed to the additional two maltose-binding sites.
About this Structure
1B90 is a Single protein structure of sequence from Bacillus cereus with , and as ligands. Active as Beta-amylase, with EC number 3.2.1.2 Full crystallographic information is available from OCA.
Reference
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose., Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S, Biochemistry. 1999 Jun 1;38(22):7050-61. PMID:10353816
Page seeded by OCA on Thu Feb 21 11:52:47 2008
Categories: Bacillus cereus | Beta-amylase | Single protein | Adachi, M. | Kage, T. | Mikami, B. | Nanmori, T. | Sarikaya, E. | Shinke, R. | Utsumi, S. | ACT | CA | SO4 | Hydrolase(o-glycosyl)
