4RZH

Crystal structure of FabG from Synechocystis sp. PCC 6803

Summary for 4RZH

• Entry DOI: 10.2210/pdb4rzh/pdb
• Related: 4RZI
• Descriptor: 3-oxoacyl-[acyl-carrier protein] reductase (2 entities in total)
• Functional Keywords: short-chain dehydrogenase/reductase (sdr) family, keto-acyl reductase, oxidoreductase
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 2
• Total formula weight: 51487.36

Authors

Liu, Y.,Xue, S. (deposition date: 2014-12-22, release date: 2015-09-16, Last modification date: 2023-09-20)

Primary citation

Liu, Y.,Feng, Y.,Cao, X.,Li, X.,Xue, S.
Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803.
Febs Lett., 589:3052-3057, 2015

PubMed Abstract: PhaB (acetoacetyl-CoA reductase) catalyzes the reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA in polyhydroxybutyrate (PHB) synthesis and FabG (3-ketoacyl-acyl-carrier-protein reductase) catalyzes the β-ketoacyl-ACP to yield (R)-3-hydroxyacyl-ACP in fatty acid biosynthesis. Both of them have been classified into the same group EC 1.1.1. PhaB is limited with substrate specificities, while FabG was considered as a potential PhaB due to broad substrate selectivity despite of low activity. Here, X-ray crystal structures of FabG and PhaB from the photosynthetic microorganism Synechocystis sp. PCC 6803 were resolved. Based on them, a high-performance FabG on acyl-CoA directed by structural evolution was constructed that may serve as a critical enzyme to partition carbon flow from fatty acid synthesis to PHA.

PubMed: 26358291
DOI: 10.1016/j.febslet.2015.09.001

Experimental method

X-RAY DIFFRACTION (2.2 Å)