2zus | pdb_00002zus

Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase

spinqualitylabelsall models 2zus, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zus is a 4 chain structure with sequence from Bifidobacterium longum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Related: 2zut, 2zuu, 2zuv, 2zuw Gene: lnpA (Bifidobacterium longum) Activity: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase, with EC number 2.4.1.211 Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q5NU17_BIFLO] Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold.,Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, Fushinobu S J Biol Chem. 2009 Mar 13;284(11):7273-83. Epub 2009 Jan 5. PMID:19124470 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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