2REJ
ABC-transporter choline binding protein in unliganded semi-closed conformation
Summary for 2REJ
| Entry DOI | 10.2210/pdb2rej/pdb |
| Related | 2REG 2RF1 2RIN |
| Descriptor | PUTATIVE GLYCINE BETAINE ABC TRANSPORTER PROTEIN (1 entity in total) |
| Functional Keywords | type ii binding protein, aromatic box, abc-transporter, transport protein, choline-binding protein |
| Biological source | Rhizobium meliloti (Sinorhizobium meliloti) |
| Total number of polymer chains | 2 |
| Total formula weight | 64604.03 |
| Authors | Oswald, C.,Smits, S.H.J.,Hoeing, M.,Sohn-Boeser, L.,Le Rudulier, D.,Schmitt, L.,Bremer, E. (deposition date: 2007-09-26, release date: 2008-09-16, Last modification date: 2024-11-13) |
| Primary citation | Oswald, C.,Smits, S.H.,Hoing, M.,Sohn-Bosser, L.,Dupont, L.,Le Rudulier, D.,Schmitt, L.,Bremer, E. Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states. J.Biol.Chem., 283:32848-32859, 2008 Cited by PubMed Abstract: The ATP-binding cassette transporter ChoVWX is one of several choline import systems operating in Sinorhizobium meliloti. Here fluorescence-based ligand binding assays were used to quantitate substrate binding by the periplasmic ligand-binding protein ChoX. These data confirmed that ChoX recognizes choline and acetylcholine with high and medium affinity, respectively. We also report the crystal structures of ChoX in complex with either choline or acetylcholine. These structural investigations revealed an architecture of the ChoX binding pocket and mode of substrate binding similar to that reported previously for several compatible solute-binding proteins. Additionally the ChoX-acetylcholine complex permitted a detailed structural comparison with the carbamylcholine-binding site of the acetylcholine-binding protein from the mollusc Lymnaea stagnalis. In addition to the two liganded structures of ChoX, we were also able to solve the crystal structure of ChoX in a closed, substrate-free conformation that revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. This structure is only the second of its kind and raises the important question of how ATP-binding cassette transporters are capable of distinguishing liganded and unliganded-closed states of the binding protein. PubMed: 18779321DOI: 10.1074/jbc.M806021200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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