Member database | CDD |
CDD type | domain |
Short name | PBP2_OpuAC_like |
Set | Periplasmic_Binding_Protein_Type_2 |
Description
References
1.Adaptation of Escherichia coli to high osmolarity environments: osmoregulation of the high-affinity glycine betaine transport system proU. Lucht JM, Bremer E. FEMS Microbiol Rev 14, 3-20, (1994). PMID: 8011357
2.Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states. Oswald C, Smits SH, Hoing M, Sohn-Bosser L, Dupont L, Le Rudulier D, Schmitt L, Bremer E. J. Biol. Chem. 283, 32848-59, (2008). View articlePMID: 18779321
3.Proteins with similar architecture exhibit similar large-scale dynamic behavior. Keskin O, Jernigan RL, Bahar I. Biophys J 78, 2093-106, (2000). PMID: 10733987
4.Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. Fukami-Kobayashi K, Tateno Y, Nishikawa K. J. Mol. Biol. 286, 279-90, (1999). View articlePMID: 9931266
5.The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. Felder CB, Graul RC, Lee AY, Merkle HP, Sadee W. AAPS PharmSci 1, E2, (1999). PMID: 11741199
6.The osmoprotectant proline betaine is a major substrate for the binding-protein-dependent transport system ProU of Escherichia coli K-12. Haardt M, Kempf B, Faatz E, Bremer E. Mol. Gen. Genet. 246, 783-6, (1995). View articlePMID: 7898450
7.Biochemical and structural analysis of the Bacillus subtilis ABC transporter OpuA and its isolated subunits. Horn C, Jenewein S, Sohn-Bosser L, Bremer E, Schmitt L. J. Mol. Microbiol. Biotechnol. 10, 76-91, (2005). View articlePMID: 16645306
8.Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Tam R, Saier MH Jr. Microbiol. Rev. 57, 320-46, (1993). View articlePMID: 8336670