1GRR

CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-Nac-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE

1GRR の概要

• エントリーDOI: 10.2210/pdb1grr/pdb
• 関連するPDBエントリー: 1GRQ 1QHN 1QHS 1QHX 1QHY
• 分子名称: CHLORAMPHENICOL 3-O PHOSPHOTRANSFERASE, SULFATE ION, N-ACETYL-P-NITROPHENYLSERINOL, ... (4 entities in total)
• 機能のキーワード: transferase, kinase, antibiotic resistance, phosphorylation, mononucleotide binding fold
• 由来する生物種: STREPTOMYCES VENEZUELAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19184.67

構造登録者

Izard, T. (登録日: 2001-12-15, 公開日: 2002-01-04, 最終更新日: 2023-12-13)

主引用文献

Izard, T.
Structural Basis for Chloramphenicol Tolerance in Streptomyces Venezuelae by Chloramphenicol Phosphotransferase Activity
Protein Sci., 10:1508-, 2001

PubMed Abstract: Streptomyces venezuelae synthesizes chloramphenicol (Cm), an inhibitor of ribosomal peptidyl transferase activity, thereby inhibiting bacterial growth. The producer escapes autoinhibition by its own secondary metabolite through phosphorylation of Cm by chloramphenicol phosphotransferase (CPT). In addition to active site binding, CPT binds its product 3-phosphoryl-Cm, in an alternate product binding site. To address the mechanisms of Cm tolerance of the producer, the crystal structures of CPT were determined in complex with either the nonchlorinated Cm (2-N-Ac-Cm) at 3.1 A resolution or the antibiotic's immediate precursor, the p-amino analog p-NH(2)-Cm, at 2.9 A resolution. Surprisingly, p-NH(2)-Cm binds CPT in a novel fashion. Additionally, neither 2-N-Ac-Cm nor p-NH(2)-Cm binds to the secondary product binding site.

PubMed: 11468347
DOI: 10.1110/PS.10.8.1508

実験手法

X-RAY DIFFRACTION (2.9 Å)