1LR0

Pseudomonas aeruginosa TolA Domain III, Seleno-methionine Derivative

Summary for 1LR0

• Entry DOI: 10.2210/pdb1lr0/pdb
• Descriptor: TolA protein, ZINC ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: domain-swapping, tola, tonb, protein transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell inner membrane; Single-pass type II membrane protein (Potential): P50600
• Total number of polymer chains: 1
• Total formula weight: 14869.73

Authors

Witty, M.,Sanz, C.,Shah, A.,Grossman, J.G.,Mizuguchi, K.,Perham, R.N.,Luisi, B. (deposition date: 2002-05-14, release date: 2002-05-29, Last modification date: 2024-10-30)

Primary citation

Witty, M.,Sanz, C.,Shah, A.,Grossmann, J.G.,Mizuguchi, K.,Perham, R.N.,Luisi, B.
Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein.
EMBO J., 21:4207-4218, 2002

PubMed Abstract: The crystal structure of the C-terminal domain III of Pseudomonas aeruginosa TolA has been determined at 1.9 A resolution. The fold is similar to that of the corresponding domain of Escherichia coli TolA, despite the limited amino acid sequence identity of the two proteins (20%). A pattern was discerned that conserves the fold of domain III within the wider TolA family and, moreover, reveals a relationship between TolA domain III and the C-terminal domain of the TonB transporter proteins. We propose that the TolA and TonB C-terminal domains have a common evolutionary origin and are related by means of domain swapping, with interesting mechanistic implications. We have also determined the overall shape of the didomain, domains II + III, of P.aeruginosa TolA by solution X-ray scattering. The molecule is monomeric-its elongated, stalk shape can accommodate the crystal structure of domain III at one end, and an elongated helical bundle within the portion corresponding to domain II. Based on these data, a model for the periplasmic domains of P.aeruginosa TolA is presented that may explain the inferred allosteric properties of members of the TolA family. The mechanisms of TolA-mediated entry of bateriophages in P.aeruginosa and E.coli are likely to be similar.

PubMed: 12169623
DOI: 10.1093/emboj/cdf417

Experimental method

X-RAY DIFFRACTION (1.914 Å)