1GCG
THE 1.9 ANGSTROMS X-RAY STRUCTURE OF A CLOSED UNLIGANDED FORM OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUM
Summary for 1GCG
Entry DOI | 10.2210/pdb1gcg/pdb |
Descriptor | GALACTOSE/GLUCOSE-BINDING PROTEIN, CALCIUM ION (3 entities in total) |
Functional Keywords | galactose-binding protein |
Biological source | Salmonella typhimurium |
Cellular location | Periplasm: P23905 |
Total number of polymer chains | 1 |
Total formula weight | 33500.74 |
Authors | Flocco, M.M.,Mowbray, S.L. (deposition date: 1994-02-03, release date: 1994-05-31, Last modification date: 2024-02-07) |
Primary citation | Flocco, M.M.,Mowbray, S.L. The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J.Biol.Chem., 269:8931-8936, 1994 Cited by PubMed Abstract: The three-dimensional structure of a ligand-free closed form of the glucose/galactose binding protein from Salmonella typhimurium has been determined at a resolution of 1.9 A. The crystallographic R-factor for the refined structure is 17.9%. The model contains all the atoms of the 309 residues of the protein sequence, a calcium ion, and 174 water molecules. The root mean square (r.m.s.) deviations for the whole molecule are: 0.010 A for bond lengths and 2.44 degrees for bond angles, indicating a good stereochemistry for the model. This structure shows that the protein is able to close in the absence of ligand, adopting a conformation similar to the liganded form but slightly more open. Water molecules satisfy the hydrogen bonding ability of the hydrophilic side chains of the binding site in a manner which is reminiscent of the sugars' hydrogen-bonding patterns. Since packing forces are weak, the crystallization event is unlikely to trigger a change from an open to a closed conformation. Instead, the latter must be one of the species in equilibrium in solution which is selected by packing in the crystal lattice. PubMed: 8132630PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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