@article{
 title = {Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125},
 type = {article},
 year = {2005},
 identifiers = {[object Object]},
 volume = {280},
 id = {07598f04-d993-3569-bee2-e9083d951833},
 created = {2018-02-28T22:42:48.339Z},
 file_attached = {false},
 profile_id = {a39b8b7f-45f4-3d11-94d2-dbc38be2487d},
 last_modified = {2018-02-28T22:42:48.339Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {true},
 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 β-anomeric hydroxyl configuration from the α-anomer or 1-deoxyxylose. We have determined the crystal structures of Rex in unliganded and complex forms at 1.35-2.20-Å 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 α 10 . His-319 in this loop forms a direct hydrogen bond with the β-hydroxyl of xylose at subsite +1, contributing to the specific recognition of anomers at the reducing end. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.},
 bibtype = {article},
 author = {Fushinobu, S. and Hidaka, M. and Honda, Y. and Wakagi, T. and Shoun, H. and Kitaoka, M.},
 journal = {Journal of Biological Chemistry},
 number = {17}
}

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