1b90: Difference between revisions

Revision as of 12:52, 21 February 2008

BACILLUS CEREUS BETA-AMYLASE APO FORM

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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-[[Image:1b90.gif|left|200px]]<br /><applet load="1b90" size="450" color="white" frame="true" align="right" spinBox="true"
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 '''BACILLUS CEREUS BETA-AMYLASE APO FORM'''<br />
 ==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.
+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==
-B90 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B90 OCA].
+B90 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==
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 [[Category: hydrolase(o-glycosyl)]]
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