Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ye Y,Saburi W,Odaka R,Kato K,Sakurai N,Komoda K,Nishimoto M,Kitaoka M,Mori H,Yao Mdoi
10.1002/1873-3468.12105subject
Has Abstractpub_date
2016-03-01 00:00:00pages
828-37issue
6eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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