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| | <StructureSection load='6jzu' size='340' side='right'caption='[[6jzu]], [[Resolution|resolution]] 2.18Å' scene=''> | | <StructureSection load='6jzu' size='340' side='right'caption='[[6jzu]], [[Resolution|resolution]] 2.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jzu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JZU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jzu]] 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=6JZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JZU FirstGlance]. <br> |
| - | </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=OCD:OCTADECANAL'>OCD</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.181Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Synpcc7942_1594, SEC0028 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2]), SEC0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</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=OCD:OCTADECANAL'>OCD</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Long-chain_acyl-[acyl-carrier-protein]_reductase Long-chain acyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.80 1.2.1.80] </span></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=6jzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzu OCA], [https://pdbe.org/6jzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jzu RCSB], [https://www.ebi.ac.uk/pdbsum/6jzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzu OCA], [http://pdbe.org/6jzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jzu RCSB], [http://www.ebi.ac.uk/pdbsum/6jzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/Q8KPT4_SYNE7 Q8KPT4_SYNE7]] Catalyzes the decarbonylation of fatty aldehydes to alkanes.[HAMAP-Rule:MF_00931] | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anacystis nidulans r2]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gao, Y]] | + | [[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] |
| - | [[Category: Li, M]] | + | [[Category: Gao Y]] |
| - | [[Category: Zhang, H M]] | + | [[Category: Li M]] |
| - | [[Category: Aldehyde]] | + | [[Category: Zhang HM]] |
| - | [[Category: Alkane]]
| + | |
| - | [[Category: Oxidoreductase-lyase complex]]
| + | |
| - | [[Category: Oxygenase]]
| + | |
| - | [[Category: Reductase]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB. Microbial biosynthesis of alkanes. Science. 2010 Jul 30;329(5991):559-62. doi: 10.1126/science.1187936. PMID:20671186 doi:10.1126/science.1187936
- ↑ 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. 2020 Mar 23;11(1):1525. doi: 10.1038/s41467-020-15268-y. PMID:32251275 doi:http://dx.doi.org/10.1038/s41467-020-15268-y
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