This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6jzq
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6jzq' size='340' side='right'caption='[[6jzq]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='6jzq' size='340' side='right'caption='[[6jzq]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6jzq]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZQ OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6jzq]] is a 5 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=6JZQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JZQ FirstGlance]. <br> |
| - | </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> | + | </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])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <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'>[http://proteopedia.org/fgij/fg.htm?mol=6jzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzq OCA], [http://pdbe.org/6jzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jzq RCSB], [http://www.ebi.ac.uk/pdbsum/6jzq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzq 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/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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6jzq" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Anacystis nidulans r2]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gao, Y]] | [[Category: Gao, Y]] | ||
Revision as of 06:00, 22 April 2020
The crystal structure of acyl-acyl carrier protein (acyl-ACP) reductase (AAR)
| |||||||||||
Categories: Anacystis nidulans r2 | Large Structures | Gao, Y | Li, M | Zhang, H M | Aldehyde | Alkane | Oxidoreductase | Oxygenase | Reductase
