The structural basis of sequence-independent peptide binding by OppA protein.

Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities.

[1]  P. Kraulis.  A program to produce both detailed and schematic plots of protein structures , 1991 .

[2]  Long-Fei Wu,et al.  The nik operon of Escherichia coli encodes a periplasmic binding‐protein‐dependent transport system for nickel , 1993, Molecular microbiology.

[3]  R. Poorman,et al.  Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein , 1991, Journal of bacteriology.

[4]  C. Higgins,et al.  Crystallization of the periplasmic oligopeptide-binding protein of Salmonella typhimurium. , 1988, Journal of molecular biology.

[5]  C. Higgins,et al.  Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide‐binding protein , 1991, Molecular microbiology.

[6]  G. F. Ames.  Bacterial periplasmic transport systems: structure, mechanism, and evolution. , 1986, Annual review of biochemistry.

[7]  T. Bergfors,et al.  Structural basis of pilus subunit recognition by the PapD chaperone. , 1993, Science.

[8]  M. A. Saper,et al.  The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens , 1987, Nature.

[9]  L. Larsson,et al.  A new class of synthetic antibacterials acting on lipopolysaccharide biosynthesis , 1987, Nature.

[10]  C. Slaughter,et al.  The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species , 1992, Infection and immunity.

[11]  C. Higgins,et al.  Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein. , 1986, European journal of biochemistry.

[12]  R. Read.  Improved Fourier Coefficients for Maps Using Phases from Partial Structures with Errors , 1986 .

[13]  F. Quiocho.  Atomic structures and function of periplasmic receptors for active transport and chemotaxis , 1991 .

[14]  C. Higgins,et al.  Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli , 1987, Journal of bacteriology.

[15]  C. Higgins.  Synthesizing designer drugs , 1987, Nature.

[16]  D. R. Madden,et al.  The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation , 1991, Nature.

[17]  W. Hendrickson.  Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. , 1991, Science.

[18]  C. A. Guyer,et al.  Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli , 1986, Journal of bacteriology.

[19]  J. Pandit,et al.  Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. , 1994, The Journal of biological chemistry.

[20]  S. Mowbray,et al.  1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli. , 1992, Journal of molecular biology.

[21]  B. Ames,et al.  Illicit transport: the oligopeptide permease. , 1973, Proceedings of the National Academy of Sciences of the United States of America.