5GX6

Crystal structure of solute-binding protein complexed with unsaturated chondroitin disaccharide with a sulfate group at C-4 position of GalNAc

Summary for 5GX6

• Entry DOI: 10.2210/pdb5gx6/pdb
• Related: 5GX7 5GX8
• Descriptor: Extracellular solute-binding protein family 1, 4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid-(1-3)-2-acetamido-2-deoxy-4-O-sulfo-beta-D-galactopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: glycosaminoglycan, abc transporter, solute-binding protein, sugar binding protein
• Biological source: Streptobacillus moniliformis DSM 12112
• Total number of polymer chains: 3
• Total formula weight: 168165.49

Authors

Oiki, S.,Mikami, B.,Murata, K.,Hashimoto, W. (deposition date: 2016-09-15, release date: 2017-07-26, Last modification date: 2023-11-08)

Primary citation

Oiki, S.,Mikami, B.,Maruyama, Y.,Murata, K.,Hashimoto, W.
A bacterial ABC transporter enables import of mammalian host glycosaminoglycans
Sci Rep, 7:1069-1069, 2017

PubMed Abstract: Glycosaminoglycans (GAGs), such as hyaluronan, chondroitin sulfate, and heparin, constitute mammalian extracellular matrices. The uronate and amino sugar residues in hyaluronan and chondroitin sulfate are linked by 1,3-glycoside bond, while heparin contains 1,4-glycoside bond. Some bacteria target GAGs as means of establishing colonization and/or infection, and bacterial degradation mechanisms of GAGs have been well characterized. However, little is known about the bacterial import of GAGs. Here, we show a GAG import system, comprised of a solute-binding protein (Smon0123)-dependent ATP-binding cassette (ABC) transporter, in the pathogenic Streptobacillus moniliformis. A genetic cluster responsible for depolymerization, degradation, and metabolism of GAGs as well as the ABC transporter system was found in the S. moniliformis genome. This bacterium degraded hyaluronan and chondroitin sulfate with an expression of the genetic cluster, while heparin repressed the bacterial growth. The purified recombinant Smon0123 exhibited an affinity with disaccharides generated from hyaluronan and chondroitin sulfate. X-ray crystallography indicated binding mode of Smon0123 to GAG disaccharides. The purified recombinant ABC transporter as a tetramer (Smon0121-Smon0122/Smon0120-Smon0120) reconstructed in liposomes enhanced its ATPase activity in the presence of Smon0123 and GAG disaccharides. This is the first report that has molecularly depicted a bacterial import system of both sulfated and non-sulfated GAGs.

PubMed: 28432302
DOI: 10.1038/s41598-017-00917-y

Experimental method

X-RAY DIFFRACTION (1.81 Å)