3FLA

RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 1

Summary for 3FLA

• Entry DOI: 10.2210/pdb3fla/pdb
• Related: 3FLB
• Descriptor: RifR, CHLORIDE ION (3 entities in total)
• Functional Keywords: alpha-beta hydrolase thioesterase, hydrolase
• Biological source: Amycolatopsis mediterranei (Nocardia mediterranei)
• Total number of polymer chains: 2
• Total formula weight: 59284.11

Authors

Smith, J.L.,Akey, D.L. (deposition date: 2008-12-18, release date: 2009-01-06, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)