9JQF

Crystal structure of the CJ0600 protein from Campylobacter jejuni

Summary for 9JQF

• Entry DOI: 10.2210/pdb9jqf/pdb
• Descriptor: 1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, SULFATE ION (3 entities in total)
• Functional Keywords: plp-dependent lyase, lyase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 1
• Total formula weight: 34534.59

Authors

Ki, D.U.,Choi, H.J.,Song, W.S.,Yoon, S.I. (deposition date: 2024-09-27, release date: 2024-11-06)

Primary citation

Ki, D.U.,Choi, H.J.,Song, W.S.,Yoon, S.I.
Structural analysis of the CJ0600 protein from Campylobacter jejuni.
Biochem.Biophys.Res.Commun., 735:150810-150810, 2024

PubMed Abstract: The Campylobacter jejuni bacterium, which causes foodborne enteritis in humans, expresses the uncharacterized protein CJ0600. Based on sequence analysis, CJ0600 has been proposed to function as a 1-aminocyclopropane-1-carboxylate (ACC) deaminase (AccDA) or cysteine desulfhydrase (CysDS). However, it has never been investigated whether CJ0600 exerts AccDA or CysDS activity or how CJ0600 mediates its enzymatic activity. To reveal the structural features necessary for the function of CJ0600, we determined the crystal structure of CJ0600 and characterized its enzymatic activity. CJ0600 contains two domains and features an interdomain pocket, which accommodates a pyridoxal 5'-phosphate (PLP) molecule as a Schiff base with its lysine residue (K35), as observed in its structural homologs, including AccDA, CysDS, and serine deaminase (SerDA). However, unlike its structural homologs, CJ0600 exists as a monomer and exhibits unique structural features throughout its structure. Moreover, CJ0600 contains unique active site residues that are not observed in AccDA, CysDS, or SerDA. Consistently, phylogenetic analysis indicates that CJ0600 and its orthologs are evolutionarily distinct from AccDA, CysDS, and SerDA. Indeed, CJ0600 showed no CysDS or SerDA activity and extremely weak AccDA activity. These observations suggest that CJ0600 functions as a unique PLP-dependent enzyme that has not been reported.

PubMed: 39418773
DOI: 10.1016/j.bbrc.2024.150810

Experimental method

X-RAY DIFFRACTION (1.7 Å)