4A10

Apo-structure of 2-octenoyl-CoA carboxylase reductase CinF from streptomyces sp.

4A10 の概要

• エントリーDOI: 10.2210/pdb4a10/pdb
• 関連するPDBエントリー: 4A0S
• 分子名称: OCTENOYL-COA REDUCTASE/CARBOXYLASE (2 entities in total)
• 機能のキーワード: oxidoreductase, ccr, pks building blocks, rossmann fold
• 由来する生物種: STREPTOMYCES SP.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 192122.08

構造登録者

Quade, N.,Huo, L.,Rachid, S.,Heinz, D.W.,Muller, R. (登録日: 2011-09-13, 公開日: 2011-12-07, 最終更新日: 2023-12-20)

主引用文献

Quade, N.,Huo, L.,Rachid, S.,Heinz, D.W.,Muller, R.
Unusual Carbon Fixation Giving Rise to Diverse Polyketide Extender Units
Nat.Chem.Biol., 8:117-, 2011

PubMed Abstract: Polyketides are structurally diverse and medically important natural products that have various biological activities. During biosynthesis, chain elongation uses activated dicarboxylic acid building blocks, and their availability therefore limits side chain variation in polyketides. Recently, the crotonyl-CoA carboxylase-reductase (CCR) class of enzymes was identified in primary metabolism and was found to be involved in extender-unit biosynthesis of polyketides. These enzymes are, in theory, capable of forming dicarboxylic acids that show any side chain from the respective unsaturated fatty acid precursor. To our knowledge, we here report the first crystal structure of a CCR, the hexylmalonyl-CoA synthase from Streptomyces sp. JS360, in complex with its substrate. Structural analysis and biochemical characterization of the enzyme, including active site mutations, are reported. Our analysis reveals how primary metabolic CCRs can evolve to produce various dicarboxylic acid building blocks, setting the stage to use CCRs for the production of unique extender units and, consequently, altered polyketides.

PubMed: 22138621
DOI: 10.1038/NCHEMBIO.734

実験手法

X-RAY DIFFRACTION (2.25 Å)