4IMP

The missing linker: a dimerization motif located within polyketide synthase modules

4IMP の概要

• エントリーDOI: 10.2210/pdb4imp/pdb
• 分子名称: Polyketide synthase extender modules 3-4, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: dimerization element, transferase
• 由来する生物種: Saccharopolyspora spinosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 249379.98

構造登録者

Zheng, J.,Keatinge-Clay, A.T. (登録日: 2013-01-03, 公開日: 2013-03-27, 最終更新日: 2023-09-20)

主引用文献

Zheng, J.,Fage, C.D.,Demeler, B.,Hoffman, D.W.,Keatinge-Clay, A.T.
The missing linker: a dimerization motif located within polyketide synthase modules.
Acs Chem.Biol., 8:1263-1270, 2013

PubMed Abstract: The dimerization of multimodular polyketide synthases is essential for their function. Motifs that supplement the contacts made by dimeric polyketide synthase enzymes have previously been characterized outside the boundaries of modules, at the N- and C-terminal ends of polyketide synthase subunits. Here we describe a heretofore uncharacterized dimerization motif located within modules. The dimeric state of this dimerization element was elucidated through the 2.6 Å resolution crystal structure of a fragment containing a dimerization element and a ketoreductase. The solution structure of a standalone dimerization element was revealed by nuclear magnetic resonance spectroscopy to be consistent with that of the crystal structure, and its dimerization constant was measured through analytical ultracentrifugation to be ∼20 μM. The dimer buries ∼990 Å(2) at its interface, and its C-terminal helices rigidly connect to ketoreductase domains to constrain their locations within a module. These structural restraints permitted the construction of a common type of polyketide synthase module.

PubMed: 23489133
DOI: 10.1021/cb400047s

実験手法

X-RAY DIFFRACTION (2.57 Å)