2xn2

Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose

spinqualitylabelsall models 2xn2, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xn2 is a 1 chain structure with sequence from Lactobacillus acidophilus NCFM. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: GLA, GOL, IMD, SME Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MELA_LACAC Hydrolyzes the short-chain alpha-galactosaccharide raffinose. Publication Abstract from PubMed Lactobacillus acidophilus NCFM is a probiotic bacterium known for its beneficial effects on human health. The importance of alpha-galactosidases (alpha-Gals) for growth of probiotic organisms on oligosaccharides of the raffinose family present in many foods is increasingly recognized. Here, the crystal structure of alpha-Gal from L. acidophilus NCFM (LaMel36A) of glycoside hydrolase (GH) family 36 (GH36) is determined by single-wavelength anomalous dispersion. In addition, a 1.58-A-resolution crystallographic complex with alpha-d-galactose at substrate binding subsite -1 was determined. LaMel36A has a large N-terminal twisted beta-sandwich domain, connected by a long alpha-helix to the catalytic (beta/alpha)(8)-barrel domain, and a C-terminal beta-sheet domain. Four identical monomers form a tightly packed tetramer where three monomers contribute to the structural integrity of the active site in each monomer. Structural comparison of LaMel36A with the monomeric Thermotoga maritima alpha-Gal (TmGal36A) reveals that O2 of alpha-d-galactose in LaMel36A interacts with a backbone nitrogen in a glycine-rich loop of the catalytic domain, whereas the corresponding atom in TmGal36A is from a tryptophan side chain belonging to the N-terminal domain. Thus, two distinctly different structural motifs participate in substrate recognition. The tetrameric LaMel36A furthermore has a much deeper active site than the monomeric TmGal36A, which possibly modulates substrate specificity. Sequence analysis of GH36, inspired by the observed structural differences, results in four distinct subgroups having clearly different active-site sequence motifs. This novel subdivision incorporates functional and architectural features and may aid further biochemical and structural analyses within GH36. Crystal Structure of alpha-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding.,Fredslund F, Abou Hachem M, Jonsgaard Larsen R, Gerd Sorensen P, Coutinho PM, Lo Leggio L, Svensson B J Mol Biol. 2011 Jul 30. PMID:21827767 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactosidase 3D structures

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