6C9U

Crystal structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase in complex with antibody fragment (Fab)

Summary for 6C9U

• Entry DOI: 10.2210/pdb6c9u/pdb
• Descriptor: 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Light chain of Fab 1B2, Heavy chain of Fab 1B2, ... (6 entities in total)
• Functional Keywords: debs, pks, polyketide synthase, 6-deoxyerthronolide b synthase, fab, antibody, phage display, transferase-immune system complex, transferase/immune system
• Biological source: Saccharopolyspora erythraea (Streptomyces erythraeus); More
• Total number of polymer chains: 3
• Total formula weight: 152046.27

Authors

Deis, L.N.,Li, X.,Mathews, I.I.,Khosla, C. (deposition date: 2018-01-28, release date: 2018-05-23, Last modification date: 2024-11-13)

Primary citation

Li, X.,Sevillano, N.,La Greca, F.,Deis, L.,Liu, Y.C.,Deller, M.C.,Mathews, I.I.,Matsui, T.,Cane, D.E.,Craik, C.S.,Khosla, C.
Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.
J. Am. Chem. Soc., 140:6518-6521, 2018

PubMed Abstract: Catalytic modules of assembly-line polyketide synthases (PKSs) have previously been observed in two very different conformations-an "extended" architecture and an "arch-shaped" architecture-although the catalytic relevance of neither has been directly established. By the use of a fully human naïve antigen-binding fragment (F) library, a high-affinity antibody was identified that bound to the extended conformation of a PKS module, as verified by X-ray crystallography and tandem size-exclusion chromatography-small-angle X-ray scattering (SEC-SAXS). Kinetic analysis proved that this antibody-stabilized module conformation was fully competent for catalysis of intermodular polyketide chain translocation as well as intramodular polyketide chain elongation and functional group modification of a growing polyketide chain. Thus, the extended conformation of a PKS module is fully competent for all of its essential catalytic functions.

PubMed: 29762030
DOI: 10.1021/jacs.8b02100

Experimental method

X-RAY DIFFRACTION (2.09 Å)