journal menu
![[Figure 5]](jc5037fig5mag.jpg)
|
|
Figure 5
Structural comparison of VhGlcNAcase with other bacterial GH20 structures in cartoon representation. (a) The structural domains of four related GH20 enzymes: VhGlcNAcase in complex with GlcNAc (PDB entry 6ezs), SpHex in complex with GlcNAc (PDB entry 1m01), SmChb in complex with (GlcNAc)2 (PDB entry 1qbb) and OfHex in complex with TMG-chitotriomycin (PDB entry 3vtr), are shown in the same orientation. (b) The molecular surfaces around the active sites are colored by the electrostatic potential calculated from the crystal structures with PyMOL. The active sites of all four structures are very acidic (red surface) and form more or less deep clefts to accommodate the oligosaccharides. Each structure is in the same orientation and the substrates of VhGlcNAcase (GlcNAc or NAG-thiazoline), SpHex (GlcNAc) and OfHex (TMG-chitotriomyocin) are superimposed with (GlcNAc)2 from the SmChb structure in the bottom right picture. |
![[Figure 5]](jc5037fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
