5bca

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{{STRUCTURE_5bca| PDB=5bca | SCENE= }}
{{STRUCTURE_5bca| PDB=5bca | SCENE= }}
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'''BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES'''
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===BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES===
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==Overview==
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The crystal structure of beta-amylase from Bacillus cereus var. mycoides was determined by the multiple isomorphous replacement method. The structure was refined to a final R-factor of 0.186 for 102,807 independent reflections with F/sigma(F) &gt; or = 2.0 at 2.2 A resolution with root-mean-square deviations from ideality in bond lengths, and bond angles of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds into three domains; the first one is the N-terminal catalytic domain with a (beta/alpha)8 barrel, the second one is the excursion part from the first one, and the third one is the C-terminal domain with two almost anti-parallel beta-sheets. The active site cleft, including two putative catalytic residues (Glu172 and Glu367), is located on the carboxyl side of the central beta-sheet in the (beta/alpha)8 barrel, as in most amylases. The active site structure of the enzyme resembles that of soybean beta-amylase with slight differences. One calcium ion is bound per molecule far from the active site. The C-terminal domain has a fold similar to the raw starch binding domains of cyclodextrin glycosyltransferase and glucoamylase.
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{{ABSTRACT_PUBMED_10348915}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Raw-starch binding domain]]
[[Category: Raw-starch binding domain]]
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Revision as of 10:56, 3 July 2008

Template:STRUCTURE 5bca

BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES

Template:ABSTRACT PUBMED 10348915

About this Structure

5BCA is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

Reference

Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution., Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y, J Biochem. 1999 Jun;125(6):1120-30. PMID:10348915

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