6B2S

Crystal structure of Xanthomonas campestris OleA H285N

Summary for 6B2S

• Entry DOI: 10.2210/pdb6b2s/pdb
• Descriptor: 3-oxoacyl-[ACP] synthase III, GLYCEROL, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: thiolase, transferase, olea, condensation
• Biological source: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
• Total number of polymer chains: 2
• Total formula weight: 78509.16

Authors

Jensen, M.R.,Goblirsch, B.R.,Esler, M.A.,Christenson, J.K.,Mohamed, F.A.,Wackett, L.P.,Wilmot, C.M. (deposition date: 2017-09-20, release date: 2018-02-28, Last modification date: 2024-10-16)

Primary citation

Jensen, M.R.,Goblirsch, B.R.,Esler, M.A.,Christenson, J.K.,Mohamed, F.A.,Wackett, L.P.,Wilmot, C.M.
The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.
FEBS Lett., 592:987-998, 2018

PubMed Abstract: Renewable production of hydrocarbons is being pursued as a petroleum-independent source of commodity chemicals and replacement for biofuels. The bacterial biosynthesis of long-chain olefins represents one such platform. The process is initiated by OleA catalyzing the condensation of two fatty acyl-coenzyme A substrates to form a β-keto acid. Here, the mechanistic role of the conserved His285 is investigated through mutagenesis, activity assays, and X-ray crystallography. Our data demonstrate that His285 is required for product formation, influences the thiolase nucleophile Cys143 and the acyl-enzyme intermediate before and after transesterification, and orchestrates substrate coordination as a defining component of an oxyanion hole. As a consequence, His285 plays a key role in enabling a mechanistic strategy in OleA that is distinct from other thiolases.

PubMed: 29430657
DOI: 10.1002/1873-3468.13004

Experimental method

X-RAY DIFFRACTION (2 Å)