EC Number   |
Reference |
|---|
   7.6.2.9 | by hanging-drop method, structures of substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution, structures show a substrate-binding protein-dependent-typical class II fold, structural differences of complexes occur within the ligand-binding pocket as well as across the domain-domain interface, explaining the differences in affinity of the substrate-binding domain-glycine betaine complex with KD = 0.017 mM, and substrate-binding domain-proline betaine complex with KD = 0.295 mM |
675375 |
| 7.6.2.9 | crystallization in an open and closed-liganded conformation, to 1.9 and 2.3 A resolution, respectively. Solutes like proline and carnitine bind with affinities that are 3 to 4 orders of magnitude lower than affinities of substrates glycine betaine or proline betaine. The low affinity substrates are not noticeably transported by membrane-reconstituted OpuA. The binding pocket is formed by three tryptophans coordinating the quaternary ammonium group of glycine betaine in the closed-liganded structure |
720807 |
| 7.6.2.9 | OpuBC protein crystal structure analysis, PDB ID 3R6U |
750650 |
| 7.6.2.9 | substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution |
675495 |
| 7.6.2.9 | substrate-binding protein OpuBC in complex with choline, to 1.6 A resolution. The positively charged trimethylammonium head group of choline is wedged into an aromatic cage formed by four tyrosine residues and is bound via cation-pi interactions. The hydroxyl group of choline protrudes out of this aromatic cage and makes a single interaction with residue Gln19. A water network stabilizes choline within its substrate-binding site and promotes indirect interactions between the two lobes of the OpuBC protein. Disruption of this intricate water network strongly reduces choline binding affinity or abrogates ligand binding |
720258 |
| 7.6.2.9 | substrate-binding protein OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine to 2.3, 2.7, 2.4, 1.9 and 2.1 A resolution, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with a substrate-binding pocket located at the interdomain cleft. Upon substrate binding, the two domains shift towards each other to trap the substrate |
718785 |
