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![[Figure 1]](jc5037fig1mag.jpg)
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Figure 1
Domain organization and overall crystal structure of VhGlcNAcase. (a) Domain composition of the VhGlcNAcase sequence. (b) Topology diagram of VhGlcNAcase analyzed with the PDBSum server. The carbohydrate-binding domain (residues 1–114) is represented in dark pink, the α+β domain (residues 148–259) in blue and the (β/α)8 TIM-barrel catalytic domain (residues 292–633) in green. Eight β-strands are labeled β1–β8 and the six regular α-helices connecting the β-strands are labeled α1–α8. Short helices are depicted by cylinders labeled η. Segmented secondary-structure elements are denoted α′, for instance α2′ indicates the short helix within the region of the α2 helix. (c) Ribbon representation of the overall structure of VhGlcNAcase, consisting of three domains. The N-terminal carbohydrate-binding (CBD) domain is presented in dark pink, the α+β domain is in blue, a linker between the CBD domain and the α+β domain is in gray and the TIM-barrel catalytic (Cat) domain is in green. The GlcNAc molecule in the active site of VhGlcNAcase is shown as a black ball-and-stick model with C atoms in black, N atoms in blue and O atoms in red. |
![[Figure 1]](jc5037fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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