journal menu
![[Figure 7]](jc5037fig7mag.jpg)
|
|
Figure 7
Comparison of substrate specificity based on the 3D structures of VhGlcNAcase and exo-β-N-acetylglucosaminidase from S. pneumoniae (StrH). (a) Ribbon representation of VhGlcNAcase (green and black) superimposed with StrH (PDB entry 2yla; pale pink and dark pink), showing the different orientations of the three long loops depicted as L2, L3 and L7 for VhGlcNAcase and L2′, L3′ and L7′ for StrH. The NAG in the active site of VhGlcNAcase is represented by a black ball-and-stick model, whereas the NGA2B in the active site of StrH is represented by a white ball-and-stick model. (b) Superposition of VhGlcNAcase (green surface) complexed with GlcNAc (black ball-and-stick model) and StrH complexed with NGA2B (white ball-and-stick model), showing a putative steric clash of NGA2B due to Trp546 and Ala547 on loop 7 (L7) if it were bound to VhGlcNAcase. The position of loop L7 (black loops in VhGlcNAcase) close to the active site narrows the substrate-binding pocket in VhGlcNAcase. |
![[Figure 7]](jc5037fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
