1WU5
Crystal structure of reducing-end-xylose releasing exo-oligoxylanase complexed with xylose
Summary for 1WU5
Entry DOI | 10.2210/pdb1wu5/pdb |
Related | 1WU4 1WU6 |
Descriptor | xylanase Y, beta-D-xylopyranose, NICKEL (II) ION, ... (5 entities in total) |
Functional Keywords | (alpla/alpha)6 barrel, glycoside hydrolase family 8, hydrolase |
Biological source | Bacillus halodurans |
Total number of polymer chains | 1 |
Total formula weight | 46429.72 |
Authors | Fushinobu, S.,Hidaka, M.,Honda, Y.,Wakagi, T.,Shoun, H.,Kitaoka, M. (deposition date: 2004-12-01, release date: 2005-02-22, Last modification date: 2023-10-25) |
Primary citation | Fushinobu, S.,Hidaka, M.,Honda, Y.,Wakagi, T.,Shoun, H.,Kitaoka, M. Structural Basis for the Specificity of the Reducing End Xylose-releasing Exo-oligoxylanase from Bacillus halodurans C-125 J.Biol.Chem., 280:17180-17186, 2005 Cited by PubMed Abstract: Reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125 (Rex) hydrolyzes xylooligosaccharides whose degree of polymerization is greater than or equal to 3, releasing the xylose unit at the reducing end. It is a unique exo-type glycoside hydrolase that recognizes the xylose unit at the reducing end in a very strict manner, even discriminating the beta-anomeric hydroxyl configuration from the alpha-anomer or 1-deoxyxylose. We have determined the crystal structures of Rex in unliganded and complex forms at 1.35-2.20-A resolution and revealed the structural aspects of its three subsites ranging from -2 to +1. The structure of Rex was compared with those of endo-type enzymes in glycoside hydrolase subfamily 8a (GH-8a). The catalytic machinery of Rex is basically conserved with other GH-8a enzymes. However, subsite +2 is blocked by a barrier formed by a kink in the loop before helix alpha10. His-319 in this loop forms a direct hydrogen bond with the beta-hydroxyl of xylose at subsite +1, contributing to the specific recognition of anomers at the reducing end. PubMed: 15718242DOI: 10.1074/jbc.M413693200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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