6I3G

Crystal structure of a putative peptide binding protein AppA from Clostridium difficile

Summary for 6I3G

• Entry DOI: 10.2210/pdb6i3g/pdb
• Descriptor: ABC transporter, substrate-binding protein, family 5, IODIDE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: abc transporter, solute binding protein, appa, peptide binding protein
• Biological source: Clostridioides difficile
• Total number of polymer chains: 1
• Total formula weight: 55497.81

Authors

Hughes, A.M.,Wilkinson, A.,Dodson, E. (deposition date: 2018-11-06, release date: 2019-04-10, Last modification date: 2024-05-15)

Primary citation

Hughes, A.,Wilson, S.,Dodson, E.J.,Turkenburg, J.P.,Wilkinson, A.J.
Crystal structure of the putative peptide-binding protein AppA from Clostridium difficile.
Acta Crystallogr.,Sect.F, 75:246-253, 2019

PubMed Abstract: Peptides play an important signalling role in Bacillus subtilis, where their uptake by one of two ABC-type oligopeptide transporters, Opp and App, is required for efficient sporulation. Homologues of these transporters in Clostridium difficile have been characterized, but their role, and hence that of peptides, in regulating sporulation in this organism is less clear. Here, the oligopeptide-binding receptor proteins for these transporters, CdAppA and CdOppA, have been purified and partially characterized, and the crystal structure of CdAppA has been determined in an open unliganded form. Peptide binding to either protein could not be observed in Thermofluor assays with a set of ten peptides of varying lengths and compositions. Re-examination of the protein sequences together with structure comparisons prompts the proposal that CdAppA is not a versatile peptide-binding protein but instead may bind a restricted set of peptides. Meanwhile, CdOppA is likely to be the receptor protein for a nickel-uptake system.

PubMed: 30950825
DOI: 10.1107/S2053230X1900178X

Experimental method

X-RAY DIFFRACTION (2 Å)