6phx

SpAga D472N structure in complex with raffinose

spinqualitylabelsall models 6phx, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6phx is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ACT, EDO, FRU, GLA, GLC, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2URQ6_STRPN Publication Abstract from PubMed Streptococcus pneumoniae is an opportunistic respiratory pathogen that can spread to other body sites, including the ears, brain and blood. The ability of this bacterium to breakdown, import and metabolize a wide range of glycans is key to its virulence. Intriguingly, S. pneumoniae can utilize several plant oligosaccharides for growth in vitro, including raffinose-family oligosaccharides (RFOs, which are alpha-(1-->6)-galactosyl extensions of sucrose). An RFO utilization locus has been identified in the pneumococcal genome; however, none of the proteins encoded by this locus have been biochemically characterized. The enigmatic ability of S. pneumoniae to utilize RFOs has recently received attention as mutations in two of the RFO locus genes have been linked to the tissue tropism of clinical pneumococcal isolates. Here, we use functional studies combined with X-ray crystallography to show that, while the pneumococcal RFO locus encodes for all the machinery required for uptake and degradation of RFOs, the individual pathway components are biochemically inefficient. We also demonstrate that the initiating enzyme in this pathway, the alpha-galactosidase Aga (a family 36 glycoside hydrolase), can cleave alpha-(1-->3)-linked galactose units from a linear blood group antigen. We propose that the pneumococcal RFO pathway is an evolutionary relic that is not utilized in this streptococcal species and, as such, is under no selection pressure to maintain binding affinity and/or catalytic efficiency. We speculate that the apparent contribution of RFO utilization to pneumococcal tissue tropism may, in fact, be due to the essential role the ATPase RafK plays in the transport of other carbohydrates. Molecular analysis of an enigmatic Streptococcus pneumoniae virulence factor: the raffinose-family oligosaccharide utilization system.,Hobbs JK, Meier EPW, Pluvinage B, Mey MA, Boraston AB J Biol Chem. 2019 Oct 7. pii: RA119.010280. doi: 10.1074/jbc.RA119.010280. PMID:31591266 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactosidase 3D structures

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