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==Crystal structure of AAR with NADPH and stearyl in complex with ADO binding a long chain carbohydrate==
<StructureSection load='6jzy' size='340' side='right'caption='[[6jzy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jzy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JZY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=OCD:OCTADECANAL'>OCD</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzy OCA], [https://pdbe.org/6jzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jzy RCSB], [https://www.ebi.ac.uk/pdbsum/6jzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AAR_SYNE7 AAR_SYNE7] Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase.<ref>PMID:20671186</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Structural insights into catalytic mechanism and product delivery of cyanobacterial acyl-acyl carrier protein reductase.,Gao Y, Zhang H, Fan M, Jia C, Shi L, Pan X, Cao P, Zhao X, Chang W, Li M Nat Commun. 2020 Mar 23;11(1):1525. doi: 10.1038/s41467-020-15268-y. PMID:32251275<ref>PMID:32251275</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jzy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
[[Category: Gao Y]]
[[Category: Li M]]
[[Category: Zhang HM]]