cd14748

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold

CDD entry
Member databaseCDD
CDD typedomain
Short namePBP2_UgpB
SetPeriplasmic_Binding_Protein_Type_2

Description

This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
[2, 5, 6, 4, 1, 3]

References

1.Maltose transport system of Escherichia coli: an ABC-type transporter. Nikaido H. FEBS Lett 346, 55-8, (1994). PMID: 8206159

2.Determinants of substrate specificity and biochemical properties of the sn-glycerol-3-phosphate ATP binding cassette transporter (UgpB-AEC2 ) of Escherichia coli. Wuttge S, Bommer M, Jager F, Martins BM, Jacob S, Licht A, Scheffel F, Dobbek H, Schneider E. Mol. Microbiol. 86, 908-20, (2012). View articlePMID: 23013274

3.The dynamics of the MBP-MalFGK(2) interaction: a prototype for binding protein dependent ABC-transporter systems. Shilton BH. Biochim Biophys Acta 1778, 1772-80, (2008). PMID: 17950243

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.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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