Crystal Structure and Catalytic Mechanism of PglD from Campylobacter jejuni
The carbohydrate 2, 4-diacetamido-2, 4, 6-trideoxy-{alpha}-d-glucopyranose (BacAc2) 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-a-d-glucopyranose (UDP-4-amino-sugar) to form UDP-BacAc2. 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.
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 980092
- Report Number(s):
- BNL-93010-2010-JA; JBCHA3; TRN: US201015%%1477
- Journal Information:
- Journal of Biological Chemistry, Vol. 283, Issue 41; ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
ALANINES
CARBOHYDRATES
CATALYSIS
COENZYMES
CRYSTAL STRUCTURE
DATA
ENZYMES
FUNCTIONALS
LINERS
MUTANTS
PATHOGENS
PROTEINS
RESIDUES
STRUCTURAL CHEMICAL ANALYSIS
SUBSTRATES
national synchrotron light source