3KG7

Dehydratase domain from CurH module of Curacin polyketide synthase

3KG7 の概要

• エントリーDOI: 10.2210/pdb3kg7/pdb
• 関連するPDBエントリー: 3KG6 3KG8 3KG9
• 分子名称: CurH (2 entities in total)
• 機能のキーワード: polyketide synthase, double hotdog fold, dehydratase, lyase
• 由来する生物種: Lyngbya majuscula
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 131792.88

構造登録者

Akey, D.L.,Smith, J.L. (登録日: 2009-10-28, 公開日: 2010-01-19, 最終更新日: 2024-10-09)

主引用文献

Akey, D.L.,Razelun, J.R.,Tehranisa, J.,Sherman, D.H.,Gerwick, W.H.,Smith, J.L.
Crystal Structures of Dehydratase Domains from the Curacin Polyketide Biosynthetic Pathway.
Structure, 18:94-105, 2010

PubMed Abstract: Modular polyketide synthases (PKS) make novel natural products through a series of preprogrammed chemical steps catalyzed by an assembly line of multidomain modules. Each assembly-line step involves unique extension and modification reactions, resulting in tremendous diversity of polyketide products. Dehydratase domains catalyze formation of an alpha,beta-double bond in the nascent polyketide intermediate. We present crystal structures of the four dehydratase domains from the curacin A PKS. The catalytic residues and substrate binding site reside in a tunnel within a single monomer. The positions of the catalytic residues and shape of the substrate tunnel explain how chirality of the substrate hydroxyl group may determine the configuration of the product double bond. Access to the active site may require opening the substrate tunnel, forming an open trench. The arrangement of monomers within the dimer is consistent among PKS dehydratases and differs from that seen in the related mammalian fatty acid synthases.

PubMed: 20152156
DOI: 10.1016/j.str.2009.10.018

実験手法

X-RAY DIFFRACTION (2.77 Å)