6JZQ

The crystal structure of acyl-acyl carrier protein (acyl-ACP) reductase (AAR)

Summary for 6JZQ

• Entry DOI: 10.2210/pdb6jzq/pdb
• Descriptor: Long-chain acyl-[acyl-carrier-protein] reductase (2 entities in total)
• Functional Keywords: reductase, alkane, aldehyde, oxygenase, oxidoreductase
• Biological source: Synechococcus elongatus PCC 7942
• Total number of polymer chains: 5
• Total formula weight: 191558.54

Authors

Zhang, H.M.,Li, M.,Gao, Y. (deposition date: 2019-05-03, release date: 2020-04-01, Last modification date: 2024-03-27)

Primary citation

Gao, Y.,Zhang, H.,Fan, M.,Jia, C.,Shi, L.,Pan, X.,Cao, P.,Zhao, X.,Chang, W.,Li, M.
Structural insights into catalytic mechanism and product delivery of cyanobacterial acyl-acyl carrier protein reductase.
Nat Commun, 11:1525-1525, 2020

PubMed Abstract: Long-chain alk(a/e)nes represent the major constituents of conventional transportation fuels. Biosynthesis of alkanes is ubiquitous in many kinds of organisms. Cyanobacteria possess two enzymes, acyl-acyl carrier protein (acyl-ACP) reductase (AAR) and aldehyde-deformylating oxygenase (ADO), which function in a two-step alkane biosynthesis pathway. These two enzymes act in series and possibly form a complex that efficiently converts long chain fatty acyl-ACP/fatty acyl-CoA into hydrocarbon. While the structure of ADO has been previously described, structures of both AAR and AAR-ADO complex have not been solved, preventing deeper understanding of this pathway. Here, we report a ligand-free AAR structure, and three AAR-ADO complex structures in which AARs bind various ligands. Our results reveal the binding pattern of AAR with its substrate/cofactor, and suggest a potential aldehyde-transferring channel from AAR to ADO. Based on our structural and biochemical data, we proposed a model for the complete catalytic cycle of AAR.

PubMed: 32251275
DOI: 10.1038/s41467-020-15268-y

Experimental method

X-RAY DIFFRACTION (2.798 Å)