Backbone chemical shifts assignments of D-allose binding protein in the free form and in complex with D-allose

David Castaño; Oscar Millet

doi:10.1007/s12104-010-9260-7

Backbone chemical shifts assignments of D-allose binding protein in the free form and in complex with D-allose

Biomol NMR Assign. 2011 Apr;5(1):31-4. doi: 10.1007/s12104-010-9260-7. Epub 2010 Aug 14.

Authors

David Castaño¹, Oscar Millet

Affiliation

¹ Structural Biology Unit, CICbioGUNE, Bizkaia Technology Park, Derio, Spain.

PMID: 20711759
DOI: 10.1007/s12104-010-9260-7

Abstract

D-allose binding protein (ALBP) belongs to the family of perisplamic receptors of the bacterial ABC transporter system. ALBP experiences a significant conformational rearrangement upon binding to the sugar. Here, we report the sequential backbone assignment for the ALBP from Escherichia coli in the free form (BMRB no. 16982) and in complex with D-allose (BMRB no. 16984).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

ATP-Binding Cassette Transporters / chemistry*
Escherichia coli Proteins / chemistry*
Glucose / chemistry*
Nuclear Magnetic Resonance, Biomolecular*
Protein Structure, Secondary
Temperature

Substances

ATP-Binding Cassette Transporters
D-allose binding protein, E coli
Escherichia coli Proteins
allose
Glucose