3MBP

MALTODEXTRIN-BINDING PROTEIN WITH BOUND MALTOTRIOSE

Summary for 3MBP

• Entry DOI: 10.2210/pdb3mbp/pdb
• Related PRD ID: PRD_900009
• Descriptor: MALTODEXTRIN-BINDING PROTEIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: periplasmic binding protein
• Biological source: Escherichia coli
• Cellular location: Periplasm: P02928
• Total number of polymer chains: 1
• Total formula weight: 41257.59

Authors

Spurlino, J.C.,Quiocho, F.A. (deposition date: 1997-06-25, release date: 1997-12-24, Last modification date: 2024-05-22)

Primary citation

Quiocho, F.A.,Spurlino, J.C.,Rodseth, L.E.
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.
Structure, 5:997-1015, 1997

PubMed Abstract: Active-transport processes perform a vital function in the life of a cell, maintaining cell homeostasis and allowing access of nutrients. Maltodextrin/maltose-binding protein (MBP; M(r) = 40k) is a receptor protein which serves as an initial high-affinity binding component of the active-transport system of maltooligosaccharides in bacteria. MBP also participates in chemotaxis towards maltooligosaccharides. The interaction between MBP and specific cytoplasmic membrane proteins initiates either active transport or chemotaxis. In order to gain new understanding of the function of MBP, especially its versatility in binding different linear and cyclic oligosaccharides with similar affinities, we have undertaken high-resolution X-ray analysis of three oligosaccharide-bound structures.

PubMed: 9309217
DOI: 10.1016/S0969-2126(97)00253-0

Experimental method

X-RAY DIFFRACTION (1.7 Å)