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Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 angstrom resolution
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
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1999 (English)In: JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, Vol. 286, no 5, p. 1519-1531Article in journal (Refereed) Published
Abstract [en]

ABC transport systems for import or export of nutrients and other substances across the cell membrane are widely distributed in nature. In most bacterial systems, a periplasmic component is the primary determinant of specificity of the transport complex a

Place, publisher, year, edition, pages
1999. Vol. 286, no 5, p. 1519-1531
Keywords [en]
periplasmic binding protein; ABC transport system; allose; X-ray crystallography; GALACTOSE CHEMORECEPTOR PROTEIN; X-RAY STRUCTURE; STRUCTURE REFINEMENT; SALMONELLA-TYPHIMURIUM; PERIPLASMIC RECEPTORS; MULTIDRUG RESISTANCE; MAXIMUM-LIKELIHOOD; MAMMALIAN-CE
Identifiers
URN: urn:nbn:se:uu:diva-28292OAI: oai:DiVA.org:uu-28292DiVA, id: diva2:56188
Note
Addresses: Mowbray SL, Swedish Univ Agr Sci, Biomed Ctr, Dept Mol Biol, Box 590, SE-75124 Uppsala, Sweden. Swedish Univ Agr Sci, Biomed Ctr, Dept Mol Biol, SE-75124 Uppsala, Sweden. Korea Adv Inst Sci & Technol, Dept Biol Sci, Yusong Ku, Taejon 305701, SoAvailable from: 2006-12-20 Created: 2006-12-20 Last updated: 2015-03-31

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