Journal of Molecular Biology
Article1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli☆
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SAXS/WAXS data of conformationally flexible ribose binding protein
2024, Data in BriefIn vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes
2015, Journal of Biological ChemistryCrystal structure of Sa240: A ribose pyranase homolog with partial active site from Staphylococcus aureus
2011, Journal of Structural BiologyCitation Excerpt :In solution ribose exists as a mixture of α- and β-pyranose, and α- and β-furanose, of which β-pyranose is the predominant form. Ribose in β-pyranose form can be recognized by the periplasmic ribose binding protein RbsB and imported into bacterial cells (Mowbray and Cole, 1992). Before further utilization, the ribose is phosphorylated by ribokinase RbsK.
Furanose-specific sugar transport. Characterization of a bacterial galactofuranose-binding protein
2009, Journal of Biological ChemistryCitation Excerpt :A Matthews coefficient of 2.1 Å3/Da was calculated suggesting the presence of one molecule in the asymmetric unit. The structure was solved by molecular replacement using the program PHASER (25) and the coordinates for the d-ribose-binding protein from E. coli (PDB entry code 1DBP, Ref. 26) as the search model. ARP/wARP (27) built the initial model that was completed in iterative cycles of REFMAC5 (28) and COOT (29).
ATP-binding cassette transporters in Escherichia coli
2008, Biochimica et Biophysica Acta - BiomembranesLocal Encoding of Computationally Designed Enzyme Activity
2007, Journal of Molecular Biology
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The later portions of the work were supported by a grant from the Swedish Natural Science Research Council to S.L.M. (K-KU 9991-300).
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Present address: Biocryst Inc., University of Alabama, 1075 13th Ave. S.,Birmingham, AL 35205, USA