4NA2

Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to its natural intermediate

Summary for 4NA2

• Entry DOI: 10.2210/pdb4na2/pdb
• Related: 2HG4 2QO3 4NA1 4NA3
• Descriptor: Polyketide synthase PksJ (2 entities in total)
• Functional Keywords: condensing enzyme fold, transferase
• Biological source: Bacillus subtilis subsp. subtilis
• Cellular location: Cytoplasm: P40806
• Total number of polymer chains: 2
• Total formula weight: 141194.38

Authors

Gay, D.C.,Gay, G.R.,Keatinge-Clay, A.T. (deposition date: 2013-10-21, release date: 2014-02-19, Last modification date: 2023-09-20)

Primary citation

Gay, D.C.,Gay, G.,Axelrod, A.J.,Jenner, M.,Kohlhaas, C.,Kampa, A.,Oldham, N.J.,Piel, J.,Keatinge-Clay, A.T.
A close look at a ketosynthase from a trans-acyltransferase modular polyketide synthase.
Structure, 22:444-451, 2014

PubMed Abstract: The recently discovered trans-acyltransferase modular polyketide synthases catalyze the biosynthesis of a wide range of bioactive natural products in bacteria. Here we report the structure of the second ketosynthase from the bacillaene trans-acyltransferase polyketide synthase. This 1.95 Å resolution structure provides the highest resolution view available of a modular polyketide synthase ketosynthase and reveals a flanking subdomain that is homologous to an ordered linker in cis-acyltransferase modular polyketide synthases. The structure of the cysteine-to-serine mutant of the ketosynthase acylated by its natural substrate provides high-resolution details of how a native polyketide intermediate is bound and helps explain the basis of ketosynthase substrate specificity. The substrate range of the ketosynthase was further investigated by mass spectrometry.

PubMed: 24508341
DOI: 10.1016/j.str.2013.12.016

Experimental method

X-RAY DIFFRACTION (2.3 Å)