4TN0

Crystal Structure of the C-terminal Periplasmic Domain of Phosphoethanolamine Transferase EptC from Campylobacter jejuni

Summary for 4TN0

• Entry DOI: 10.2210/pdb4tn0/pdb
• Descriptor: UPF0141 protein yjdB, ZINC ION (3 entities in total)
• Functional Keywords: alkaline phosphatase-like, phosphoethanolamine transferase, phosphothreonine, periplasm, transferase
• Biological source: Campylobacter jejuni subsp. jejuni HB93-13
• Total number of polymer chains: 3
• Total formula weight: 110830.66

Authors

Fage, C.D.,Brown, D.,Boll, J.M.,Keatinge-Clay, A.T.,Trent, M.S. (deposition date: 2014-06-02, release date: 2014-10-08, Last modification date: 2024-10-23)

Primary citation

Fage, C.D.,Brown, D.B.,Boll, J.M.,Keatinge-Clay, A.T.,Trent, M.S.
Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni.
Acta Crystallogr.,Sect.D, 70:2730-2739, 2014

PubMed Abstract: The foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine (pEtN). Modifying lipid A with pEtN promotes cationic antimicrobial peptide resistance, whereas post-translationally modifying the flagellar rod protein FlgG with pEtN promotes flagellar assembly and motility, which are processes that are important for intestinal colonization. EptC, the pEtN transferase required for all known pEtN cell-surface modifications in C. jejuni, is a predicted inner-membrane metalloenzyme with a five-helix N-terminal transmembrane domain followed by a soluble sulfatase-like catalytic domain in the periplasm. The atomic structure of the catalytic domain of EptC (cEptC) was crystallized and solved to a resolution of 2.40 Å. cEptC adopts the α/β/α fold of the sulfatase protein family and harbors a zinc-binding site. A phosphorylated Thr266 residue was observed that was hypothesized to mimic a covalent pEtN-enzyme intermediate. The requirement for Thr266 as well as the nearby residues Asn308, Ser309, His358 and His440 was ascertained via in vivo activity assays on mutant strains. The results establish a basis for the design of pEtN transferase inhibitors.

PubMed: 25286856
DOI: 10.1107/S1399004714017623

Experimental method

X-RAY DIFFRACTION (2.4 Å)