cd13639

Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; the type 2 periplasmic binding protein fold

CDD entry
Member databaseCDD
CDD typedomain
Short namePBP2_OpuAC_like
SetPeriplasmic_Binding_Protein_Type_2

Description

This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to betaine compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine and proline betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
[5, 8, 4, 3, 7, 6, 1, 2]

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

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