2fw0

Apo Open Form of Glucose/Galactose Binding Protein

spinqualitylabelsall models 2fw0, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fw0 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: CA, CIT, MLA, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MGLB_ECOLI Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (PubMed:3057628, PubMed:4927373). Chemotaxis requires MglB, but not MglA or MglC (PubMed:6294056). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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