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3WAU

Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P

Summary for 3WAU
Entry DOI10.2210/pdb3wau/pdb
Related3WAS 3WAT 4KMI
Descriptor4-O-beta-D-mannosyl-D-glucose phosphorylase, PHOSPHATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
Functional Keywords5-bladed beta propeller fold, phosphorylase, mannan biodegradation, transferase
Biological sourceBacteroides fragilis
Total number of polymer chains2
Total formula weight89015.78
Authors
Nakae, S.,Ito, S.,Higa, M.,Senoura, T.,Wasaki, J.,Hijikata, A.,Shionyu, M.,Ito, S.,Shirai, T. (deposition date: 2013-05-08, release date: 2013-09-04, Last modification date: 2023-11-08)
Primary citationNakae, S.,Ito, S.,Higa, M.,Senoura, T.,Wasaki, J.,Hijikata, A.,Shionyu, M.,Ito, S.,Shirai, T.
Structure of Novel Enzyme in Mannan Biodegradation Process 4-O-beta-d-Mannosyl-d-Glucose Phosphorylase MGP
J.Mol.Biol., 425:4468-4478, 2013
Cited by
PubMed Abstract: The crystal structure of a novel component of the mannan biodegradation system, 4-O-β-D-mannosyl-D-glucose phosphorylase (MGP), was determined to a 1.68-Å resolution. The structure of the enzyme revealed a unique homohexameric structure, which was formed by using two helices attached to the N-terminus and C-terminus as a tab for sticking between subunits. The structures of MGP complexes with genuine substrates, 4-O-β-D-mannosyl-D-glucose and phosphate, and the product D-mannose-1-phosphate were also determined. The complex structures revealed that the invariant residue Asp131, which is supposed to be the general acid/base, did not exist close to the glycosidic Glc-O4 atom, which should be protonated in the catalytic reaction. Also, no solvent molecule that might mediate a proton transfer from Asp131 was observed in the substrate complex structure, suggesting that the catalytic mechanism of MGP is different from those of known disaccharide phosphorylases.
PubMed: 23954514
DOI: 10.1016/j.jmb.2013.08.002
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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数据于2024-11-13公开中

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