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Figure 3 | Aquatic Biosystems

Figure 3

From: Function and biotechnology of extremophilic enzymes in low water activity

Figure 3

Structural features of an extremophilic glucose dehydrogenase. The protein structure (PDB ID:2B5V) [30] was downloaded from RCSB Protein Data Bank [123] and illustrated using DeepView Swiss-PdbViewer [124]. (A) Ribbon structure is shown with one subunit colored light gray and one subunit colored dark gray. Boxed region encompassing three α-helices of one subunit and two partial α-helices of the other subunit are shown in detail in part B. Acidic residues (aspartic acid and glutamic acid) are colored red and pink respectively, and basic residues (arginine and lysine) are colored dark blue and medium blue, respectively. Water molecules are colored light purple. (B) Expanded region showing a portion with side chains of exposed acidic residues and buried basic residues. Asterisk indicates residues of the dark gray subunit. An inter-subunit ion pair between Arg289 of one subunit and Asp277 of the other subunit is shown by a line labeled 2.62 Å, the distance between interacting atoms of the two residues.

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