Towards the molecular mechanism of Na(+)/solute symport in prokaryotes.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Author(s): Jung H;Jung H
  • Source:
    Biochimica et biophysica acta [Biochim Biophys Acta] 2001 May 01; Vol. 1505 (1), pp. 131-43.
  • Publication Type:
    Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam : Elsevier Pub. Co.
    • Subject Terms:
      Amino Acid Transport Systems, Neutral* ; Escherichia coli Proteins* ; Symporters*; Bacterial Proteins/*metabolism ; Carrier Proteins/*metabolism ; Sodium/*metabolism; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Cations, Monovalent ; Cytoplasm/metabolism ; Escherichia coli/metabolism ; Ligands ; Models, Chemical ; Molecular Sequence Data ; Periplasm/metabolism ; Proline/metabolism ; Protein Conformation
    • Abstract:
      The Na(+)/solute symporter family (SSF, TC No. 2.A.21) contains more than 40 members of pro- and eukaryotic origin. Besides their sequence similarity, the transporters share the capability to utilize the free energy stored in electrochemical Na(+) gradients for the accumulation of solutes. As part of catabolic pathways most of the transporters are most probably involved in the acquisition of nutrients. Some transporters play a role in osmoadaptation. With a high resolution structure still missing, a combination of genetic, protein chemical and spectroscopic methods has been used to gain new insights into the structure and molecular mechanism of action of the transport proteins. The studies suggest a common 13-helix motif for all members of the SSF according to which the N-terminus is located in the periplasm and the C-terminus is directed into the cytoplasm (except for proteins containing a N- or C-terminal extension). Furthermore, an amino acid substitution analysis of the Na(+)/proline transporter (PutP) of Escherichia coli, a member of the SSF, has identified regions of particular functional importance. For example, amino acids of TM II of PutP proved to be critical for high affinity binding of Na(+) and proline. In addition, it was shown that ligand binding induces widespread conformational alterations in the transport protein. Taken together, the studies substantiate the common idea that Na(+)/solute symport is the result of a series of ligand-induced structural changes.
    • Number of References:
      116
    • Accession Number:
      0 (Amino Acid Transport Systems, Neutral)
      0 (Bacterial Proteins)
      0 (Carrier Proteins)
      0 (Cations, Monovalent)
      0 (Escherichia coli Proteins)
      0 (Ligands)
      0 (Symporters)
      111565-48-1 (PutP protein, E coli)
      9DLQ4CIU6V (Proline)
      9NEZ333N27 (Sodium)
    • Publication Date:
      Date Created: 20010315 Date Completed: 20010510 Latest Revision: 20190610
    • Publication Date:
      20221213
    • Accession Number:
      10.1016/s0005-2728(00)00283-8
    • Accession Number:
      11248195