View source for 5bca

[[Image:5bca.gif|left|200px]]

 {{Structure
|PDB= 5bca |SIZE=350|CAPTION= <scene name='initialview01'>5bca</scene>, resolution 2.2&Aring;
|SITE= <scene name='pdbsite=CAA:Catalytic+Residues'>CAA</scene>, <scene name='pdbsite=CAB:Catalytic+Residues'>CAB</scene>, <scene name='pdbsite=CAC:Catalytic+Residues'>CAC</scene> and <scene name='pdbsite=CAD:Catalytic+Residues'>CAD</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</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= 
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bca OCA], [http://www.ebi.ac.uk/pdbsum/5bca PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5bca RCSB]</span>
}}

'''BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES'''


==Overview==
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.

==About this Structure==
5BCA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BCA 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:[http://www.ncbi.nlm.nih.gov/pubmed/10348915 10348915]
[[Category: Bacillus cereus]]
[[Category: Beta-amylase]]
[[Category: Single protein]]
[[Category: Kishimoto, Y.]]
[[Category: Kusunoki, M.]]
[[Category: Nitta, Y.]]
[[Category: Oyama, T.]]
[[Category: Takasaki, Y.]]
[[Category: beta-amylase]]
[[Category: hydrolase]]
[[Category: raw-starch binding domain]]

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