1abe | pdb_00001abe

NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

spinqualitylabelsall models 1abe, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1abe is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entry 1abp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ARA, ARB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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