8KEM

PKS domains-fused AmpC EC2

Summary for 8KEM

• Entry DOI: 10.2210/pdb8kem/pdb
• Descriptor: SDR family NAD(P)-dependent oxidoreductase,Beta-lactamase (1 entity in total)
• Functional Keywords: trans-at pks docking domain, macrolactin, fusion protein, protein binding
• Biological source: Bacillus amyloliquefaciens; More
• Total number of polymer chains: 3
• Total formula weight: 142106.13

Authors

Son, S.Y.,Bae, D.W.,Cha, S.S. (deposition date: 2023-08-12, release date: 2024-06-05, Last modification date: 2024-09-18)

Primary citation

Son, S.Y.,Bae, D.W.,Kim, E.,Jeong, B.G.,Kim, M.Y.,Youn, S.Y.,Yi, S.,Kim, G.,Hahn, J.S.,Lee, N.K.,Yoon, Y.J.,Cha, S.S.
Structural investigation of the docking domain assembly from trans-AT polyketide synthases.
Structure, 32:1477-1487.e4, 2024

PubMed Abstract: Docking domains (DDs) located at the C- and N-termini of polypeptides play a crucial role in directing the assembly of polyketide synthases (PKSs), which are multienzyme complexes. Here, we determined the crystal structure of a complex comprising the C-terminal DD (DD) and N-terminal DD (DD) of macrolactin trans-acyltransferase (AT) PKS that were fused to a functional enzyme, AmpC EC2 β-lactamase. Interface analyses of the DD/DD complex revealed the molecular intricacies in the core section underpinning the precise DD assembly. Additionally, circular dichroism and steady-state kinetics demonstrated that the formation of the DD/DD complex had no influence on the structural and functional fidelity of the fusion partner, AmpC EC2. This inspired us to apply the DD/DD assembly to metabolon engineering. Indeed, DD assembly induced the formation of a complex between 4-coumarate-CoA ligase and chalcone synthase both involved in flavonoid biosynthesis, leading to a remarkable increase in naringenin production in vitro.

PubMed: 38908377
DOI: 10.1016/j.str.2024.05.017

Experimental method

X-RAY DIFFRACTION (2.76998285856 Å)