Structural highlights
Function
[ARAF_ECOLI] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tertiary structure refinement at 1.7 A resolution of the liganded form of L-arabinose-binding protein from Escherichia coli has revealed a novel binding site geometry which accommodates both alpha- and beta-anomers of L-arabinose. This detailed structure analysis provides new understanding of protein-sugar interaction, the process by which the binding protein minimizes the difference in the stability of the two bound sugar anomers, and the roles of periplasmic binding proteins in active transport.
Novel stereospecificity of the L-arabinose-binding protein.,Quiocho FA, Vyas NK Nature. 1984 Aug 2-8;310(5976):381-6. PMID:6379466[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Quiocho FA, Vyas NK. Novel stereospecificity of the L-arabinose-binding protein. Nature. 1984 Aug 2-8;310(5976):381-6. PMID:6379466
