5AYC

Crystal structure of Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) in complexes with sulfate and 4-O-beta-D-mannosyl-D-glucose

Summary for 5AYC

• Entry DOI: 10.2210/pdb5ayc/pdb
• Related: 5AY9 5AYD 5AYE
• Descriptor: 4-O-beta-D-mannosyl-D-glucose phosphorylase, beta-D-mannopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: glycoside hydrolase family 130, transferase
• Biological source: Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7)
• Total number of polymer chains: 1
• Total formula weight: 44138.36

Authors

Ye, Y.,Saburi, W.,Kato, K.,Yao, M. (deposition date: 2015-08-13, release date: 2016-03-23, Last modification date: 2024-03-20)

Primary citation

Ye, Y.,Saburi, W.,Odaka, R.,Kato, K.,Sakurai, N.,Komoda, K.,Nishimoto, M.,Kitaoka, M.,Mori, H.,Yao, M.
Structural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamilies.
Febs Lett., 590:828-837, 2016

PubMed 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.

PubMed: 26913570
DOI: 10.1002/1873-3468.12105

Experimental method

X-RAY DIFFRACTION (1.9 Å)