6JZU
The crystal structure of acyl-acyl carrier protein (acyl-ACP) reductase (AAR) in complex with aldehyde deformylating oxygenase (ADO)
Summary for 6JZU
| Entry DOI | 10.2210/pdb6jzu/pdb |
| Descriptor | Long-chain acyl-[acyl-carrier-protein] reductase, Aldehyde decarbonylase, octadecanal, ... (6 entities in total) |
| Functional Keywords | reductase, alkane, aldehyde, oxygenase, oxidoreductase-lyase complex, oxidoreductase/lyase |
| Biological source | Synechococcus elongatus PCC 7942 More |
| Total number of polymer chains | 2 |
| Total formula weight | 67138.41 |
| Authors | Zhang, H.M.,Li, M.,Gao, Y. (deposition date: 2019-05-03, release date: 2020-04-01, Last modification date: 2024-10-09) |
| 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 Cited by 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: 32251275DOI: 10.1038/s41467-020-15268-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.181 Å) |
Structure validation
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