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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Beta-amylase from bacillus cereus var. Mycoides
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Structure:
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Protein (1,4-alpha-d-glucan maltohydrolase.). Chain: a, b, c, d. Ec: 3.2.1.2
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Source:
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Bacillus cereus. Organism_taxid: 1396. Strain: bacillus cereus. Variant: mycoides. Cellular_location: extracellular
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Resolution:
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2.20Å
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R-factor:
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0.186
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R-free:
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0.240
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Authors:
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T.Oyama,M.Kusunoki,Y.Kishimoto,Y.Takasaki,Y.Nitta
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Key ref:
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T.Oyama
et al.
(1999).
Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution.
J Biochem (tokyo),
125,
1120-1130.
PubMed id:
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Date:
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12-Mar-99
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Release date:
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15-Mar-00
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PROCHECK
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Headers
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References
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Q9Z4N9
(Q9Z4N9_BACCE) -
Beta-amylase (Precursor)
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Seq:
Struc:
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546 a.a.
516 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.2.1.2
- Beta-amylase.
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Reaction:
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Hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
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Gene Ontology (GO) functional annotation
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Biological process
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metabolic process
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4 terms
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Biochemical function
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catalytic activity
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7 terms
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J Biochem (tokyo)
125:1120-1130
(1999)
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PubMed id:
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Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution.
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T.Oyama,
M.Kusunoki,
Y.Kishimoto,
Y.Takasaki,
Y.Nitta.
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ABSTRACT
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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) > 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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.Christiansen,
M.Abou Hachem,
S.Janecek,
A.Viksø-Nielsen,
A.Blennow,
and
B.Svensson
(2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
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FEBS J, 276,
5006-5029.
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M.Machovic,
B.Svensson,
E.A.MacGregor,
and
S.Janecek
(2005).
A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21.
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FEBS J, 272,
5497-5513.
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Y.Mezaki,
Y.Katsuya,
M.Kubota,
and
Y.Matsuura
(2001).
Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
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Biosci Biotechnol Biochem, 65,
222-225.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
