Mutational analysis eliminates Glu64 and Glu94 as candidates for 'catalytic carboxylate' in the bacterial ATP-binding-cassette protein MalK

FEBS Lett. 1997 Aug 18;413(2):211-4. doi: 10.1016/s0014-5793(97)00913-7.

Abstract

MalK is the ATP-hydrolyzing subunit of the binding protein-dependent ATP-binding-cassette (ABC) transport system for maltose from Salmonella typhimurium. In a recent hypothesis, Glu64 and Glu94 of MalK were proposed as candidates for 'catalytic carboxylate', common to ATP- and GTP-hydrolyzing proteins [Yoshida and Amano (1995) FEBS Lett. 359, 1-5]. Substitution of both residues and, additionally, Glu74 by either glutamine or glycine and valine, respectively, had no deleterious effect on maltose transport. Thus, our data disprove the above notion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry
  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Biological Transport
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Catalysis
  • DNA Mutational Analysis*
  • Glutamic Acid / physiology*
  • Maltose / metabolism
  • Protein Structure, Secondary
  • Recombinant Fusion Proteins
  • Salmonella typhimurium / genetics
  • Salmonella typhimurium / metabolism

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Carrier Proteins
  • MalK protein, Bacteria
  • MalK protein, Salmonella typhimurium
  • Recombinant Fusion Proteins
  • Glutamic Acid
  • Maltose