This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1bfn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="1bfn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfn, resolution 2.07&Aring;" /> '''BETA-AMYLASE/BETA-CY...)
Next diff →

Revision as of 09:29, 20 November 2007

Image:1bfn.gif

1bfn, resolution 2.07Å

Drag the structure with the mouse to rotate

BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX

Overview

In order to study the interaction of soybean beta-amylase with substrate, we solved the crystal structure of beta-cyclodextrin-enzyme complex and, compared it with that of alpha-cyclodextrin-enzyme complex. The enzyme was, expressed in Escherichia coli at a high level as a soluble and, catalytically active protein. The purified recombinant enzyme had, properties nearly identical to those of native soybean beta-amylase and, formed the same crystals as the native enzyme. The crystal structure of, recombinant enzyme complexed with beta-cyclodextrin was refined at 2. 07-A, resolution with a final crystallographic R value of 15.8% (Rfree = 21.1%)., The root mean square deviation in the position of C-alpha atoms between, this recombinant enzyme and the native enzyme was 0.22 A. These results, indicate that the expression system established here is suitable for, studying structure-function relationships of beta-amylase. The, conformation of the bound beta-cyclodextrin takes an ellipsoid shape in, contrast to the circular shape of the bound alpha-cyclodextrin. The, cyclodextrins shared mainly two glucose binding sites, 3 and 4. The, glucose residue 4 was slightly shifted from the maltose binding site. This, suggests that the binding site of the cyclodextrins is important for its, holding of a cleaved substrate, which enables the multiple attack, mechanism of beta-amylase.

About this Structure

1BFN is a Single protein structure of sequence from Glycine max with SO4 as ligand. Active as Beta-amylase, with EC number 3.2.1.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin., Adachi M, Mikami B, Katsube T, Utsumi S, J Biol Chem. 1998 Jul 31;273(31):19859-65. PMID:9677422

Page seeded by OCA on Tue Nov 20 11:36:48 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bfn"
Personal tools