6ql9

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

6ql9 is a 12 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.82Å
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]

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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ql9"

@@ Line 3: / Line 3: @@
 <StructureSection load='6ql9' size='340' side='right'caption='[[6ql9]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ql9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QL9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QL9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ql9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QL9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2P:ADENOSINE-2-5-DIPHOSPHATE'>A2P</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</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]] 2.82&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=J8W:'>J8W</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2P:ADENOSINE-2-5-DIPHOSPHATE'>A2P</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=J8W:(2~{S})-2-azanyl-3-(3-oxidanyl-3-oxidanylidene-propanoyl)oxy-propanoic+acid'>J8W</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></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=6ql9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ql9 OCA], [http://pdbe.org/6ql9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ql9 RCSB], [http://www.ebi.ac.uk/pdbsum/6ql9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ql9 ProSAT]</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=6ql9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ql9 OCA], [https://pdbe.org/6ql9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ql9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ql9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ql9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FAS2_YEAST 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] [[http://www.uniprot.org/uniprot/FAS1_YEAST 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.
+[https://www.uniprot.org/uniprot/FAS2_YEAST 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]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 6ql9" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
 [[Category: Large Structures]]
-[[Category: Saccharomyces cerevisiae]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Chari, A]]
+[[Category: Chari A]]
-[[Category: Graf, B]]
+[[Category: Graf B]]
-[[Category: Linden, A]]
+[[Category: Linden A]]
-[[Category: Sautner, V]]
+[[Category: Sautner V]]
-[[Category: Singh, K]]
+[[Category: Singh K]]
-[[Category: Stark, H]]
+[[Category: Stark H]]
-[[Category: Tittmann, K]]
+[[Category: Tittmann K]]
-[[Category: Urlaub, H]]
+[[Category: Urlaub H]]
-[[Category: Acetyl transferase]]
-[[Category: Acyl carrier protein]]
-[[Category: Dehydratase]]
-[[Category: Enoyl reductase]]
-[[Category: Fatty acid synthase]]
-[[Category: Ketoreductase]]
-[[Category: Ketosynthase]]
-[[Category: Malonyl/palmitoyl transferase]]
-[[Category: Phosphopantetheine transferase]]
-[[Category: Transferase]]

6ql9

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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