TY - JOUR
T1 - Structural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamilies
AU - Ye, Yuxin
AU - Saburi, Wataru
AU - Odaka, Rei
AU - Kato, Koji
AU - Sakurai, Naofumi
AU - Komoda, Keisuke
AU - Nishimoto, Mamoru
AU - Kitaoka, Motomitsu
AU - Mori, Haruhide
AU - Yao, Min
N1 - Publisher Copyright:
© 2016 Federation of European Biochemical Societies.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2016/3/1
Y1 - 2016/3/1
N2 - In Ruminococcus albus, 4-O-β-d-mannosyl-d-glucose phosphorylase (RaMP1) and β-(1,4)-mannooligosaccharide phosphorylase (RaMP2) belong to two subfamilies of glycoside hydrolase family 130. The two enzymes phosphorolyze β-mannosidic linkages at the nonreducing ends of their substrates, and have substantially diverse substrate specificity. The differences in their mechanism of substrate binding have not yet been fully clarified. In the present study, we report the crystal structures of RaMP1 with/without 4-O-β-d-mannosyl-d-glucose and RaMP2 with/without β-(1→4)-mannobiose. The structures of the two enzymes differ at the +1 subsite of the substrate-binding pocket. Three loops are proposed to determine the different substrate specificities. One of these loops is contributed from the adjacent molecule of the oligomer structure. In RaMP1, His245 of loop 3 forms a hydrogen-bond network with the substrate through a water molecule, and is indispensible for substrate binding.
AB - In Ruminococcus albus, 4-O-β-d-mannosyl-d-glucose phosphorylase (RaMP1) and β-(1,4)-mannooligosaccharide phosphorylase (RaMP2) belong to two subfamilies of glycoside hydrolase family 130. The two enzymes phosphorolyze β-mannosidic linkages at the nonreducing ends of their substrates, and have substantially diverse substrate specificity. The differences in their mechanism of substrate binding have not yet been fully clarified. In the present study, we report the crystal structures of RaMP1 with/without 4-O-β-d-mannosyl-d-glucose and RaMP2 with/without β-(1→4)-mannobiose. The structures of the two enzymes differ at the +1 subsite of the substrate-binding pocket. Three loops are proposed to determine the different substrate specificities. One of these loops is contributed from the adjacent molecule of the oligomer structure. In RaMP1, His245 of loop 3 forms a hydrogen-bond network with the substrate through a water molecule, and is indispensible for substrate binding.
KW - 4-O-β- d -mannosyl- d -glucose phosphorylase
KW - X-ray crystallography
KW - glycoside hydro-lase family 130
KW - hydrogen bond-network
KW - substrate recognition
KW - β-1,4-mannooligosaccharide phosphorylase
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U2 - 10.1002/1873-3468.12105
DO - 10.1002/1873-3468.12105
M3 - Article
C2 - 26913570
AN - SCOPUS:84960154652
VL - 590
SP - 828
EP - 837
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 6
ER -