1XT8

Crystal Structure of Cysteine-Binding Protein from Campylobacter jejuni at 2.0 A Resolution

Summary for 1XT8

• Entry DOI: 10.2210/pdb1xt8/pdb
• Descriptor: putative amino-acid transporter periplasmic solute-binding protein, CYSTEINE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: abc transport, cysteine uptake, amino-acid transporter periplasmic solute-binding protein, campylobacter jejuni, spine, structural genomics, structural proteomics in europe, transport protein
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 2
• Total formula weight: 65234.34

Authors

Muller, A.,Thomas, G.H.,Horler, R.,Brannigan, J.A.,Blagova, E.,Levdikov, V.M.,Fogg, M.J.,Wilson, K.S.,Wilkinson, A.J.,Structural Proteomics in Europe (SPINE) (deposition date: 2004-10-21, release date: 2005-08-23, Last modification date: 2023-08-23)

Primary citation

Muller, A.,Thomas, G.H.,Horler, R.,Brannigan, J.A.,Blagova, E.,Levdikov, V.M.,Fogg, M.J.,Wilson, K.S.,Wilkinson, A.J.
An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein.
Mol.Microbiol., 57:143-155, 2005

PubMed Abstract: Campylobacter jejuni is a Gram-negative food-borne pathogen associated with gastroenteritis in humans as well as cases of the autoimmune disease Guillain-Barré syndrome. C. jejuni is asaccharolytic because it lacks an active glycolytic pathway for the use of sugars as a carbon source. This suggests an increased reliance on amino acids as nutrients and indeed the genome sequence of this organism indicates the presence of a number of amino acid uptake systems. Cj0982, also known as CjaA, is a putative extracytoplasmic solute receptor for one such uptake system as well as a major surface antigen and vaccine candidate. The crystal structure of Cj0982 reveals a two-domain protein with density in the enclosed cavity between the domains that clearly defines the presence of a bound cysteine ligand. Fluorescence titration experiments were used to demonstrate that Cj0982 binds cysteine tightly and specifically with a K(d) of approximately 10(-7) M consistent with a role as a receptor for a high-affinity transporter. These data imply that Cj0982 is the binding protein component of an ABC-type cysteine transporter system and that cysteine uptake is important in the physiology of C. jejuni.

PubMed: 15948956
DOI: 10.1111/j.1365-2958.2005.04691.x

Experimental method

X-RAY DIFFRACTION (2 Å)