7KWS
Cj1441 with NAD+ and UDP-glucose
Summary for 7KWS
| Entry DOI | 10.2210/pdb7kws/pdb |
| Descriptor | UDP-glucose 6-dehydrogenase, URIDINE-5'-DIPHOSPHATE-GLUCOSE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | dehydrogenase, polysaccharide, carbohydrate, oxidoreductase |
| Biological source | Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) |
| Total number of polymer chains | 2 |
| Total formula weight | 92757.11 |
| Authors | Riegert, A.S.,Raushel, F.M. (deposition date: 2020-12-02, release date: 2021-01-13, Last modification date: 2023-10-18) |
| Primary citation | Riegert, A.S.,Raushel, F.M. Functional and Structural Characterization of the UDP-Glucose Dehydrogenase Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni . Biochemistry, 60:725-734, 2021 Cited by PubMed Abstract: is a pathogenic organism that can cause campylobacteriosis in children and adults. Most commonly, campylobacter infection is brought on by consumption of raw or undercooked poultry, unsanitary drinking water, or pet feces. Surrounding the bacterium is a coat of sugar molecules known as the capsular polysaccharide (CPS). The capsular polysaccharide can be very diverse among the different strains of , and this diversity is considered important for evading the host immune system. Modifications to the CPS of NCTC 11168 include O-methylation, phosphoramidylation, and amidation of glucuronate with either serinol or ethanolamine. The enzymes responsible for amidation of glucuronate are currently unknown. In this study, Cj1441, an enzyme expressed from the CPS biosynthetic gene cluster in NCTC 11168, was shown to catalyze the oxidation of UDP-α-d-glucose into UDP-α-d-glucuronic acid with NAD as the cofactor. No amide products were found in an attempt to determine whether the putative thioester intermediate formed during the oxidation of UDP-glucose by Cj1441 could be captured in the presence of added amines. The three-dimensional crystal structure of Cj1441 was determined in the presence of NAD and UDP-glucose bound in the active site of the enzyme (Protein Data Bank entry 7KWS). A more thorough bioinformatic analysis of the CPS gene cluster suggests that the amidation activity is localized to the t-terminal half of Cj1438, a bifunctional enzyme that is currently annotated as a sugar transferase. PubMed: 33621065DOI: 10.1021/acs.biochem.0c00953 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
Download full validation report
