2uv8
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2uv8]] is a 6 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=2UV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UV8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2uv8]] is a 6 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=2UV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UV8 FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
- | <tr><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='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><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='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><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://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://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [http://www.ebi.ac.uk/pdbsum/2uv8 PDBsum]</span></td></tr> |
- | <table> | + | </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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 35: | Line 37: | ||
[[Category: Fatty-acyl-CoA synthase]] | [[Category: Fatty-acyl-CoA synthase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
- | [[Category: Ban, N | + | [[Category: Ban, N]] |
- | [[Category: Frick, C | + | [[Category: Frick, C]] |
- | [[Category: Jenni, S | + | [[Category: Jenni, S]] |
- | [[Category: Leibundgut, M | + | [[Category: Leibundgut, M]] |
[[Category: Acetyl transferase]] | [[Category: Acetyl transferase]] | ||
[[Category: Acyl carrier protein]] | [[Category: Acyl carrier protein]] |
Revision as of 07:55, 25 December 2014
CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION
|
Categories: Fatty-acyl-CoA synthase | Saccharomyces cerevisiae | Ban, N | Frick, C | Jenni, S | Leibundgut, M | Acetyl transferase | Acyl carrier protein | Dehydratase | Enoyl reductase | Fatty acid biosynthesis | Fatty acid synthase | Fatty acid synthesis | Hydrolase | Ketoacyl reductase | Ketoacyl synthase | Lipid synthesis | Lyase | Malonyl/palmitoyl transferase | Multifunctional enzyme | Nad | Nadp | Oxidoreductase | Phosphopantetheine | Phosphorylation | Substrate shuttling | Transferase | Yeast