This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1gub
From Proteopedia
|
HINGE-BENDING MOTION OF D-ALLOSE BINDING PROTEIN FROM ESCHERICHIA COLI: THREE OPEN CONFORMATIONS
Overview
ABC transport systems for import or export of nutrients and other, substances across the cell membrane are widely distributed in nature. In, most bacterial systems, a periplasmic component is the primary determinant, of specificity of the transport complex as a whole. We report here the, crystal structure of the periplasmic binding protein for the allose system, (ALBP) from Escherichia coli, solved at 1.8 A resolution using the, molecular replacement method. As in the other members of the family, (especially the ribose binding protein, RBP, with which it shares 35 %, sequence homology), this structure consists of two similar domains joined, by a three-stranded hinge region. The protein is believed to exist in a, dynamic equilibrium of closed and open conformations in solution which is, an ... [(full description)]
About this Structure
1GUB is a [Single protein] structure of sequence from [[1]] with NI as [ligand]. Full crystallographic information is available from [OCA].
Reference
Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution., Chaudhuri BN, Ko J, Park C, Jones TA, Mowbray SL, J Mol Biol. 1999 Mar 12;286(5):1519-31. PMID:10064713
Page seeded by OCA on Mon Oct 29 17:33:45 2007
