1gub: Difference between revisions
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Revision as of 16:14, 30 October 2007
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HINGE-BENDING MOTION OF D-ALLOSE BINDING PROTEIN FROM ESCHERICHIA COLI: THREE OPEN CONFORMATIONS
OverviewOverview
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 as a whole. We report here the, crystal structure of the periplasmic binding protein for the allose system, (ALBP) from Escherichia coli, solved at 1.8 A resolution using the, molecular replacement method. As in the other members of the family, (especially the ribose binding protein, RBP, with which it shares 35 %, sequence homology), this structure consists of two similar domains joined, by a three-stranded hinge region. The protein is believed to exist in a, dynamic equilibrium of closed and open conformations in solution which is, an ... [(full description)]
About this StructureAbout this Structure
1GUB is a [Single protein] structure of sequence from [Escherichia coli] with NI as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution., Chaudhuri BN, Ko J, Park C, Jones TA, Mowbray SL, J Mol Biol. 1999 Mar 12;286(5):1519-31. PMID:10064713
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