5xs8

Crystal structure of solute-binding protein complexed with unsaturated chondroitin disaccharide with two sulfate groups at C-4 and C-6 positions of GalNAc

spinqualitylabelsall models 5xs8, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xs8 is a 4 chain structure with sequence from Streptobacillus moniliformis DSM 12112. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.952Å Ligands: 8EX, CA, GCD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D1AWE0_STRM9 Publication Abstract from PubMed Glycosaminoglycans (GAGs), constituted by repeating uronate and amino sugar units, are major components of mammalian extracellular matrices. Some indigenous and pathogenic bacteria target GAGs for colonization to and/or infection of host mammalian cells. In Gram-negative pathogenic Streptobacillus moniliformis, the solute-binding protein (Smon0123)-dependent ATP-binding cassette (ABC) transporter incorporates unsaturated GAG disaccharides into the cytoplasm after depolymerization by polysaccharide lyase. Smon0123, composed of N and C domains, adopts either a substrate-free open or a substrate-bound closed form by approaching two domains at 47 degrees in comparison with the open form. Here we show an alternative 39 degrees -closed conformation of Smon0123 bound to unsaturated chondroitin disaccharide sulfated at the C-4 and C-6 positions of N-acetyl-d-galactosamine residue (CDelta4S6S). In CDelta4S6S-bound Smon0123, Arg204 and Lys210 around the two sulfate groups were located at different positions from those at other substrate-bound 47 degrees -closed conformations. Therefore, the two sulfate groups in CDelta4S6S shifted substrate-binding residue arrangements, causing dynamic conformational change. Smon0123 showed less affinity with CDelta4S6S than with non-sulfated and monosulfated substrates. ATPase activity of the Smon0123-dependent ABC transporter in the presence of CDelta4S6S was lower than that in the presence of other unsaturated chondroitin disaccharides, suggesting that CDelta4S6S-bound Smon0123 was unpreferable for docking with the ABC transporter. Alternative substrate-bound conformation of bacterial solute-binding protein involved in the import of mammalian host glycosaminoglycans.,Oiki S, Kamochi R, Mikami B, Murata K, Hashimoto W Sci Rep. 2017 Dec 5;7(1):17005. doi: 10.1038/s41598-017-16801-8. PMID:29208901 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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