2ZUW
Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate
Summary for 2ZUW
| Entry DOI | 10.2210/pdb2zuw/pdb |
| Related | 2ZUS 2ZUT 2ZUU 2ZUV |
| Descriptor | Lacto-N-biose phosphorylase, 2-acetamido-2-deoxy-alpha-D-glucopyranose, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | beta-alpha-barrel, tim barrel, glycosyltransferase, transferase |
| Biological source | Bifidobacterium longum |
| Total number of polymer chains | 4 |
| Total formula weight | 343556.02 |
| Authors | Hidaka, M.,Nishimoto, M.,Kitaoka, M.,Wakagi, T.,Shoun, H.,Fushinobu, S. (deposition date: 2008-10-28, release date: 2008-12-30, Last modification date: 2024-03-13) |
| Primary citation | Hidaka, M.,Nishimoto, M.,Kitaoka, M.,Wakagi, T.,Shoun, H.,Fushinobu, S. The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: A large deformation of a tim barrel scaffold J.Biol.Chem., 284:7273-7283, 2009 Cited by PubMed Abstract: Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) from Bifidobacterium longum, a key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion. GLNBP homologues are often found in human pathogenic and commensal bacteria, and their substrate specificities potentially define the nutritional acquisition ability of these microbes in their habitat. We report the crystal structures of GLNBP in five different ligand-binding forms. This is the first three-dimensional structure of glycoside hydrolase (GH) family 112. The GlcNAc- and GalNAc-bound forms provide structural insights into distinct substrate preferences of GLNBP and its homologues from pathogens. The catalytic domain consists of a partially broken TIM barrel fold that is structurally similar to a thermophilic beta-galactosidase, strongly supporting the current classification of GLNBP homologues as one of the GH families. Anion binding induces a large conformational change by rotating a half-unit of the barrel. This is an unusual example of molecular adaptation of a TIM barrel scaffold to substrates. PubMed: 19124470DOI: 10.1074/jbc.M808525200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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