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2uv8

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Revision as of 08:59, 12 September 2018

Warning: this is a large structure, and loading might take a long time or not happen at all.

Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution

Structural highlights

2uv8 is a 6 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:
NonStd Res:
Activity:	Fatty-acyl-CoA synthase, with EC number 2.3.1.86
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Warning: this is a large structure, and loading might take a long time or not happen at all.

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.

Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase.,Leibundgut M, Jenni S, Frick C, Ban N Science. 2007 Apr 13;316(5822):288-90. PMID:17431182^[1]

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

References

↑ Leibundgut M, Jenni S, Frick C, Ban N. Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase. Science. 2007 Apr 13;316(5822):288-90. PMID:17431182 doi:316/5822/288

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2uv8"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION==
+{{Large structure}}
+==Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution==
 <StructureSection load='2uv8' size='340' side='right' caption='[[2uv8]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GVL:O-[(R)-{[(3R)-4-AMINO-3-HYDROXY-2,2-DIMETHYL-4-OXOBUTYL]OXY}(HYDROXY)PHOSPHORYL]-L-SERINE'>GVL</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty-acyl-CoA_synthase Fatty-acyl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.86 2.3.1.86] </span></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=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [http://pdbe.org/2uv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [http://www.ebi.ac.uk/pdbsum/2uv8 PDBsum]</span></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=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [http://pdbe.org/2uv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [http://www.ebi.ac.uk/pdbsum/2uv8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uv8 ProSAT]</span></td></tr>
 </table>
 {{Large structure}}
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uv/2uv8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uv/2uv8_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2uv8

From Proteopedia

Revision as of 08:59, 12 September 2018

Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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