Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
The structure was elucidated in this paperNCBI PubMed ID: 33900734Publication DOI: 10.1021/acs.biochem.1c00183Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: Hazel M. Holden <hmholden
wisc.edu>; Frank M Raushel <raushel
tamu.edu>
Institutions: Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States, Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, United States, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 553706, United States
Campylobacter jejuni is the leading cause of food poisoning in the United States and Europe. The exterior cell surface of C. jejuni is coated with a capsular polysaccharide (CPS) that is essential for the maintenance and integrity of the bacterial cell wall and evasion of the host immune response. The identity and sequences of the monosaccharide components of the CPS are quite variable and dependent on the specific strain of C. jejuni. It is currently thought that the immediate precursor for the multiple variations found in the heptose moieties of the C. jejuni CPS is GDP-d-glycero-α-d-manno-heptose. In C. jejuni NCTC 11168, the heptose moiety is d-glycero-l-gluco-heptose. It has previously been shown that Cj1427 catalyzes the oxidation of GDP-d-glycero-α-d-manno-heptose to GDP-d-glycero-4-keto-α-d-lyxo-heptose using α-ketoglutarate as a cosubstrate. Cj1430 was now demonstrated to catalyze the double epimerization of this product at C3 and C5 to form GDP-d-glycero-4-keto-β-l-xylo-heptose. Cj1428 subsequently catalyzes the stereospecific reduction of this GDP-linked heptose by NADPH to form GDP-d-glycero-β-l-gluco-heptose. The three-dimensional crystal structure of Cj1430 was determined to a resolution of 1.85 Å in the presence of bound GDP-d-glycero-β-l-gluco-heptose, a product analogue. The structure shows that it belongs to the cupin superfamily. The three-dimensional crystal structure of Cj1428 was solved in the presence of NADPH to a resolution of 1.50 Å. Its fold places it into the short-chain dehydrogenase/reductase superfamily. Typically, members in this family display a characteristic signature sequence of YXXXK, with the conserved tyrosine serving a key role in catalysis. In Cj1428, this residue is a phenylalanine.
biosynthesis, heptose, capsular polysaccharides, Campylobacter jejuni
Structure type: monomer
Location inside paper: Scheme 2, Fig. 2b, compound 4
Trivial name: GDP-D-glycero-β-L-gluco-heptose
Contained glycoepitopes: IEDB_141493,IEDB_149170,IEDB_190357
Methods: 1H NMR, X-ray, kinetics assays, genetic methods, biochemical methods, UV, FPLC, cloning, crystallization, enzymatic synthesis
Biosynthesis and genetic data: Cj1427, Cj1430, Cj1428
Synthetic data: enzymatic
3D data: 3D data
Related record ID(s): 10865
NCBI Taxonomy refs (TaxIDs): 197
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There is only one chemically distinct structure:
Found 
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