3FLB

RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 2

3FLB の概要

• エントリーDOI: 10.2210/pdb3flb/pdb
• 関連するPDBエントリー: 3FLA
• 分子名称: RifR, CHLORIDE ION, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: alpha-beta hydrolase thioesterase, hydrolase
• 由来する生物種: Amycolatopsis mediterranei (Nocardia mediterranei)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29492.02

構造登録者

Smith, J.L.,Akey, D.L. (登録日: 2008-12-18, 公開日: 2009-01-06, 最終更新日: 2024-02-21)

主引用文献

Claxton, H.B.,Akey, D.L.,Silver, M.K.,Admiraal, S.J.,Smith, J.L.
Structure and Functional Analysis of RifR, the Type II Thioesterase from the Rifamycin Biosynthetic Pathway.
J.Biol.Chem., 284:5021-5029, 2009

PubMed Abstract: Two thioesterases are commonly found in natural product biosynthetic clusters, a type I thioesterase that is responsible for removing the final product from the biosynthetic complex and a type II thioesterase that is believed to perform housekeeping functions such as removing aberrant units from carrier domains. We present the crystal structure and the kinetic analysis of RifR, a type II thioesterase from the hybrid nonribosomal peptide synthetases/polyketide synthase rifamycin biosynthetic cluster of Amycolatopsis mediterranei. Steady-state kinetics show that RifR has a preference for the hydrolysis of acyl units from the phosphopantetheinyl arm of the acyl carrier domain over the hydrolysis of acyl units from the phosphopantetheinyl arm of acyl-CoAs as well as a modest preference for the decarboxylated substrate mimics acetyl-CoA and propionyl-CoA over malonyl-CoA and methylmalonyl-CoA. Multiple RifR conformations and structural similarities to other thioesterases suggest that movement of a helical lid controls access of substrates to the active site of RifR.

PubMed: 19103602
DOI: 10.1074/jbc.M808604200

実験手法

X-RAY DIFFRACTION (1.8 Å)