 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](mn5038fig4mag.jpg)
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Figure 4
Overall fold of the biological monomer of Hev b 2. (a) Ribbon representation of several superimposed plant β-glucanases: Hev b 2 (monomer A, P21; brown), banana β-1,3-glucanase (PDB entry 2cyg ; gold), barley β-1,3–1,4-glucanase (PDB entry 1aq0 ; red), barley β-1,3-glucanase (PDB entry 1ghs ; green) and potato β-1,3-glucanase (PDB entries 3ur7 and 4gz1 ; without and with carbohydrates in the active site; grey and blue, respectively). Major differences are localized in the loops indicated by arrows. Using the numbering of Hev b 2, major differences lie in loop 1 (residues 80–85), loop 2 (94–103), which includes one catalytic residue and notably comprises the Ω-like loop that is only present in Hev b 2, loop 3 (residues 195–214), which exhibits the largest differences, loop 4 (residues 247–252) and loop 5 (residues 293–295). (b) Molecular surface of monomer C (P41 crystal). Catalytic residues (Glu94 and Glu240) and putative residues involved in substrate binding are shown in the right panel. The peptide bond of Tyr144 is in a cis configuration and adopts a conformation that occludes the carbohydrate-binding groove, as shown in the left panel (monomer B, P41). |
![[Figure 4]](mn5038fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
