1. Dextranase from Penicillium minioluteum
Anna M Larsson, Rolf Andersson, Jerry Ståhlberg, Lennart Kenne, T.Alwyn Jones 
Structure 
Volume 11, Issue 9, Pages (September 2003)
DOI: /S (03)

2. Figure 1
The Structure of Dex49A Successively Colored from Red in the N Terminus to Blue in the C Terminus
The right image structure is turned 90° counterclockwise around the vertical axis, relative to the left image.
Structure  , DOI: ( /S (03) )

3. Figure 2
Topology Map of the β Sandwich Domain that Comprises the First 200 Amino Acids of the Protein
The coloring is derived from Figure 1.
Structure  , DOI: ( /S (03) )

4. Figure 3
The Side Chains of the Hydrophobic Stacking along PB2 in the Interior of the β Helix Are Shown in Gray
Two asparagines in T2 that form a short asparagine ladder and are conserved within GH 49 are shown in gold to the right. In the interface between the two domains, a large number of amino acids are conserved within the family. These are colored in gold in the upper part of the figure.
Structure  , DOI: ( /S (03) )

5. Figure 4 1H NMR Spectra of Dextran
1H NMR specra of dextran alone (A) and 18 min (B), 1.5 hr (C), and 18 hr after addition of Dex49A.
Structure  , DOI: ( /S (03) )

6. Figure 5
Isomaltose Is Hydrogen-Bonded (Black Bubbles) to Six Amino Acids in the Protein
The density is σA-weighted 2Fo − Fc map (Read, 1986) at 0.4 electrons/Å3. The O6 hydroxyl group at the nonreducing end of the sugar is hydrogen bonded to the proposed proton donor, Asp395. Two other aspartyl residues, Asp376 and Asp396, are hydrogen bonded to the water molecule that is suggested to perform the nucleophilic attack. The amino acids that are shown in gold are completely conserved within GH 49.
Structure  , DOI: ( /S (03) )

7. Figure 6
Schematic Representation of the Interaction between the Enzyme and the Ligand, Drawn by LIGPLOT (Wallace et al., 1995)
The dotted lines are hydrogen bonds or water-mediated hydrogen bonds. The separations are given in Å units.
Structure  , DOI: ( /S (03) )

8. Figure 7
The Water-Accessible Surface of the Active Site Is Shown in the Image to the Left
The isomaltose ligand is partially visible behind Tyr463. The ball and stick image to the right is shown from the same view. A tunnel is created in the active site by the interaction between the side chains of Tyr463 and Asp317. The side chains colored in gold are located in the presumed −1 and −2 subsites and are totally conserved within GH 49.
Structure  , DOI: ( /S (03) )

9. Figure 8
The Superimposed Active Sites of Dex49A (Gray) and Polygalacturonase A from E. carotovora (Green) Are Shown
The only completely conserved residues between the active sites are the aspartyl residues suggested to be involved in the catalysis and two residues in close vicinity. Gln374 in Dex49A, which is completely conserved in GH 49, substitutes Asn200 in the +1 subsite.
Structure  , DOI: ( /S (03) )

10. Figure 9 Superimposed β Helix Domains
The β helix domains of dextranase from P. minioluteum (A), polygalacturonase A from E. carotovora (B), and ι-Carrageenase from A. fortis (C) GH families 49, 28, and 82, respectively, were superimposed, and the water-accessible surfaces of the three β helices are shown from the same view. The active sites are colored in red.
Structure  , DOI: ( /S (03) )