5bca

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[[Image:5bca.gif|left|200px]]
[[Image:5bca.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 5bca |SIZE=350|CAPTION= <scene name='initialview01'>5bca</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_5bca", creates the "Structure Box" on the page.
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|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>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_5bca| PDB=5bca | SCENE= }}
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|RELATEDENTRY=
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|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>
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}}
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'''BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES'''
'''BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES'''
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[[Category: Oyama, T.]]
[[Category: Oyama, T.]]
[[Category: Takasaki, Y.]]
[[Category: Takasaki, Y.]]
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[[Category: beta-amylase]]
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[[Category: Beta-amylase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: raw-starch binding domain]]
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[[Category: Raw-starch binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:32:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:40:54 2008''
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Revision as of 19:32, 4 May 2008

Template:STRUCTURE 5bca

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) > 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 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 Page seeded by OCA on Sun May 4 22:32:05 2008

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