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Structure paper

TitleHow members of the human gut microbiota overcome the sulfation problem posed by glycosaminoglycans.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page 7037-7042, Year 2017
Publish dateFeb 21, 2012 (structure data deposition date)
AuthorsCartmell, A. / Lowe, E.C. / Basle, A. / Firbank, S.J. / Ndeh, D.A. / Murray, H. / Terrapon, N. / Lombard, V. / Henrissat, B. / Turnbull, J.E. ...Cartmell, A. / Lowe, E.C. / Basle, A. / Firbank, S.J. / Ndeh, D.A. / Murray, H. / Terrapon, N. / Lombard, V. / Henrissat, B. / Turnbull, J.E. / Czjzek, M. / Gilbert, H.J. / Bolam, D.N.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:28630303
MethodsX-ray diffraction
Resolution1.35 - 1.95 Å
Structure data

PDB-4ak1:
Structure of BT4661, a SusE-like surface located polysaccharide binding protein from the Bacteroides thetaiotaomicron heparin utilisation locus
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4ak2:
Structure of BT4661, a SusE-like surface located polysaccharide binding protein from the Bacteroides thetaiotaomicron heparin utilisation locus
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-5g2t:
BT1596 in complex with its substrate 4,5 unsaturated uronic acid alpha 1,4 D-Glucosamine-2-N, 6-O-disulfate
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5g2u:
Structure of BT1596,a 2-O GAG sulfatase
Method: X-RAY DIFFRACTION / Resolution: 1.43 Å

PDB-5g2v:
Structure of BT4656 in complex with its substrate D-Glucosamine-2-N, 6-O-disulfate.
Method: X-RAY DIFFRACTION / Resolution: 1.39 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-UAP:
4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid

ChemComp-CIT:
CITRIC ACID

ChemComp-CA:
Unknown entry

ChemComp-SGN:
2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose

ChemComp-NO3:
NITRATE ION

Source
  • bacteroides thetaiotaomicron (bacteria)
KeywordsHEPARIN-BINDING PROTEIN / HEPARAN SULPHATE / HYDROLASE / GLYCOSAMINOGLYCAN SULFATASE

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