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.

6ql6

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of Fatty acid synthase complex from Saccharomyces cerevisiae at 2.9 Angstrom

Structural highlights

6ql6 is a 12 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FAS2_YEAST] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101] [FAS1_YEAST] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.

Publication Abstract from PubMed

Fatty acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid synthesis, the growing fatty acid chain is thought to be shuttled by the dynamic acyl carrier protein domain to several enzyme active sites. Here, we report the discovery of a gamma subunit of the 2.6 megadalton alpha6-beta6S. cerevisiae FAS, which is shown by high-resolution structures to stabilize a rotated FAS conformation and rearrange ACP domains from equatorial to axial positions. The gamma subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The gamma subunit delineates the functional compartment within FAS. As a scaffold, it may be exploited to incorporate natural and designed enzymatic activities that are not present in natural FAS.

Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase.,Singh K, Graf B, Linden A, Sautner V, Urlaub H, Tittmann K, Stark H, Chari A Cell. 2020 Mar 4. pii: S0092-8674(20)30211-7. doi: 10.1016/j.cell.2020.02.034. PMID:32160528^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Singh K, Graf B, Linden A, Sautner V, Urlaub H, Tittmann K, Stark H, Chari A. Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase. Cell. 2020 Mar 4. pii: S0092-8674(20)30211-7. doi: 10.1016/j.cell.2020.02.034. PMID:32160528 doi:http://dx.doi.org/10.1016/j.cell.2020.02.034

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ql6"

@@ Line 3: / Line 3: @@
 <StructureSection load='6ql6' size='340' side='right'caption='[[6ql6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ql6]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QL6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ql6]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QL6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QL6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=J8T:[(3~{R})-4-azanyl-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl]+dihydrogen+phosphate'>J8T</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=J8T:[(3~{R})-4-azanyl-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl]+dihydrogen+phosphate'>J8T</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ql6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ql6 OCA], [http://pdbe.org/6ql6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ql6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ql6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ql6 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=6ql6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ql6 OCA], [http://pdbe.org/6ql6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ql6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ql6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ql6 ProSAT]</span></td></tr>
 </table>
 == Function ==

6ql6

From Proteopedia

Current revision

Structure of Fatty acid synthase complex from Saccharomyces cerevisiae at 2.9 Angstrom

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox