3BSW

PglD-citrate complex, from Campylobacter jejuni NCTC 11168

3BSW の概要

• エントリーDOI: 10.2210/pdb3bsw/pdb
• 関連するPDBエントリー: 2NPO 3BSS 3BSY
• 分子名称: Acetyltransferase, CITRIC ACID (3 entities in total)
• 機能のキーワード: left-hand beta helix, hexapeptide repeat, udp, acetyl coenzyme z, rossmann fold, bacillosamine, campylobacter, pgl, n-linked glycosylation, transferase
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21582.08

構造登録者

Olivier, N.B.,Imperiali, B. (登録日: 2007-12-26, 公開日: 2008-07-29, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.77 Å)