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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Imperiali, Barbara Olivier, Nelson B. |
| Description | Author Affiliation: Olivier NB ( Department of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.) |
| Abstract | The carbohydrate 2, 4-diacetamido-2, 4, 6-trideoxy-alpha-D-glucopyranose (BacAc(2)) is found in a variety of eubacterial pathogens. In Campylobacter jejuni, PglD acetylates the C4 amino group on UDP-2-acetamido-4-amino-2, 4, 6-trideoxy-alpha-D-glucopyranose (UDP-4-amino-sugar) to form UDP-BacAc(2). Sequence analysis predicts PglD to be a member of the left-handed beta helix family of enzymes. However, poor sequence homology between PglD and left-handed beta helix enzymes with existing structural data precludes unambiguous identification of the active site. The co-crystal structures of PglD in the presence of citrate, acetyl coenzyme A, or the UDP-4-amino-sugar were solved. The biological assembly is a trimer with one active site formed between two protomers. Residues lining the active site were identified, and results from functional assays on alanine mutants suggest His-125 is critical for catalysis, whereas His-15 and His-134 are involved in substrate binding. These results are discussed in the context of implications for proteins homologous to PglD in other pathogens. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 41 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-10-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Acetylglucosamine Analogs & Derivatives Acetyltransferases Chemistry Campylobacter Jejuni Enzymology Biosynthesis Metabolism Bacterial Proteins Binding Sites Physiology Catalysis Crystallography, X-Ray Protein Structure, Quaternary Protein Structure, Secondary Structural Homology, Protein Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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