1ABE

NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

Replaces:  1ABP

Summary for 1ABE

• Entry DOI: 10.2210/pdb1abe/pdb
• Descriptor: L-ARABINOSE-BINDING PROTEIN, alpha-L-arabinopyranose, beta-L-arabinopyranose, ... (4 entities in total)
• Functional Keywords: binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 33551.26

Authors

Vyas, N.K.,Quiocho, F.A. (deposition date: 1992-04-23, release date: 1993-10-31, Last modification date: 2024-02-07)

Primary citation

Quiocho, F.A.,Vyas, N.K.
Novel stereospecificity of the L-arabinose-binding protein
Nature, 310:381-386, 1984

PubMed Abstract: 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.

PubMed: 6379466
DOI: 10.1038/310381a0

Experimental method

X-RAY DIFFRACTION (1.7 Å)