5AY9: Crystal Structure Of Ruminococcus Albus 4-o-beta-d-mannosyl-d-glucose Phosphorylase (ramp1)

In Ruminococcus albus, 4-O-beta-d-mannosyl-d-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2) belong to two subfamilies of glycoside hydrolase family 130. The two enzymes phosphorolyze beta-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-beta-d-mannosyl-d-glucose and RaMP2 with/without beta-(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.
PDB ID: 5AY9Download
MMDB ID: 137650
PDB Deposition Date: 2015/8/11
Updated in MMDB: 2016/04
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 5AY9: trimeric; determined by author and by software (PISA)
Molecular Components in 5AY9
Label Count Molecule
Proteins (3 molecules)
4-o-beta-d-mannosyl-d-glucose Phosphorylase
Molecule annotation
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