2fw0
From Proteopedia
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[[Image:2fw0.gif|left|200px]] | [[Image:2fw0.gif|left|200px]] | ||
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'''Apo Open Form of Glucose/Galactose Binding Protein''' | '''Apo Open Form of Glucose/Galactose Binding Protein''' | ||
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[[Category: Forest, K T.]] | [[Category: Forest, K T.]] | ||
[[Category: Kiessling, L L.]] | [[Category: Kiessling, L L.]] | ||
| - | [[Category: | + | [[Category: Chemotaxis]] |
| - | [[Category: | + | [[Category: Ggbp]] |
| - | [[Category: | + | [[Category: Hinge]] |
| - | [[Category: | + | [[Category: Periplasmic binding protein]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:22:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:22, 4 May 2008
Apo Open Form of Glucose/Galactose Binding Protein
Overview
D-Glucose/D-Galactose-binding protein (GGBP) mediates chemotaxis toward and active transport of glucose and galactose in a number of bacterial species. GGBP, like other periplasmic binding proteins, can exist in open (ligand-free) and closed (ligand-bound) states. We report a 0.92 angstroms resolution structure of GGBP from Escherichia coli in the glucose-bound state and the first structure of an open, unbound form of GGBP (at 1.55 angstroms resolution). These structures vary in the angle between the two structural domains; the observed difference of 31 degrees arises from torsion angle changes in a three-segment hinge. A comparison with the closely related periplasmic receptors, ribose- and allose-binding proteins, shows that the GGBP hinge residue positions that undergo the largest conformational changes are different. Furthermore, the high-quality data collected for the atomic resolution glucose-bound structure allow for the refinement of specific hydrogen atom positions, the assignment of alternate side chain conformations, the first description of CO(2) trapped after radiation-induced decarboxylation, and insight into the role of the exo-anomeric effect in sugar binding. Together, these structures provide insight into how the hinge-bending movement of GGBP facilitates ligand binding, transport, and signaling.
About this Structure
2FW0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures., Borrok MJ, Kiessling LL, Forest KT, Protein Sci. 2007 Jun;16(6):1032-41. Epub 2007 May 1. PMID:17473016 Page seeded by OCA on Sun May 4 04:22:12 2008
