4KMI
Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4
Summary for 4KMI
Entry DOI | 10.2210/pdb4kmi/pdb |
Related | 3WAS 3WAT 3WAU |
Descriptor | 4-O-beta-D-mannosyl-D-glucose phosphorylase, PHOSPHATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
Functional Keywords | 5-bladed beta propeller fold, phosphorylase, mannan biodegradation, transferase |
Biological source | Bacteroides fragilis |
Total number of polymer chains | 2 |
Total formula weight | 88685.45 |
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 citation | Nakae, 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: 23954514DOI: 10.1016/j.jmb.2013.08.002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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