Structural highlights
Function
ERYA2_SACER
Publication Abstract from PubMed
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 naive antigen-binding fragment (Fab) 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.
Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.,Li X, Sevillano N, La Greca F, Deis L, Liu YC, Deller MC, Mathews II, Matsui T, Cane DE, Craik CS, Khosla C J Am Chem Soc. 2018 May 18. doi: 10.1021/jacs.8b02100. PMID:29762030[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li X, Sevillano N, La Greca F, Deis L, Liu YC, Deller MC, Mathews II, Matsui T, Cane DE, Craik CS, Khosla C. Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module. J Am Chem Soc. 2018 May 18. doi: 10.1021/jacs.8b02100. PMID:29762030 doi:http://dx.doi.org/10.1021/jacs.8b02100
