3BSY

PglD from Campylobacter jejuni, NCTC 11168, in complex with acetyl coenzyme A

Summary for 3BSY

• Entry DOI: 10.2210/pdb3bsy/pdb
• Related: 2NPO 3BSS 3BSW
• Descriptor: Acetyltransferase, ACETYL COENZYME *A (3 entities in total)
• Functional Keywords: left-hand beta helix, hexapeptide repeat, udp, acetyl coenzyme a, rossmann fold, bacillosamine, campylobacter jejuni, pgl, n-linked glycosylation, transferase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 3
• Total formula weight: 66598.58

Authors

Olivier, N.B.,Imperiali, B. (deposition date: 2007-12-26, release date: 2008-07-29, Last modification date: 2023-08-30)

Primary citation

Olivier, N.B.,Imperiali, B.
Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni.
J.Biol.Chem., 283:27937-27946, 2008

PubMed 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.

PubMed: 18667421
DOI: 10.1074/jbc.M801207200

Experimental method

X-RAY DIFFRACTION (1.8 Å)