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| | <StructureSection load='4cw4' size='340' side='right'caption='[[4cw4]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='4cw4' size='340' side='right'caption='[[4cw4]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cw4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CW4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cw5|4cw5]]</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=4cw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cw4 OCA], [https://pdbe.org/4cw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cw4 RCSB], [https://www.ebi.ac.uk/pdbsum/4cw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cw4 ProSAT]</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=4cw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cw4 OCA], [http://pdbe.org/4cw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cw4 RCSB], [http://www.ebi.ac.uk/pdbsum/4cw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cw4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/FABY_PSEAE FABY_PSEAE]] Involved in the initiation of the fatty acid biosynthesis. Catalyzes the condensation of acetyl coenzyme A (acetyl-CoA) with malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis (FAS) primer beta-acetoacetyl-ACP. It can also use short-chain acyl-CoA as substrates, including butyryl-CoA, and hexanoyl-CoA, but does not use any of the longer chain acyl-CoA substrates.<ref>PMID:22753059</ref> <ref>PMID:24145528</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Bukhari, H S.T]] | + | [[Category: Bukhari HST]] |
| - | [[Category: Jakob, R P]] | + | [[Category: Jakob RP]] |
| - | [[Category: Maier, T]] | + | [[Category: Maier T]] |
| - | [[Category: Fa]]
| + | |
| - | [[Category: Fatty acid synthase]]
| + | |
| - | [[Category: Ka]]
| + | |
| - | [[Category: Kas i/ii]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
[FABY_PSEAE] Involved in the initiation of the fatty acid biosynthesis. Catalyzes the condensation of acetyl coenzyme A (acetyl-CoA) with malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis (FAS) primer beta-acetoacetyl-ACP. It can also use short-chain acyl-CoA as substrates, including butyryl-CoA, and hexanoyl-CoA, but does not use any of the longer chain acyl-CoA substrates.[1] [2]
Publication Abstract from PubMed
Fungal fatty acid synthase (fFAS) is a key paradigm for the evolution of complex multienzymes. Its 48 functional domains are embedded in a matrix of scaffolding elements, which comprises almost 50% of the total sequence and determines the emergent multienzymes properties of fFAS. Catalytic domains of fFAS are derived from monofunctional bacterial enzymes, but the evolutionary origin of the scaffolding elements remains enigmatic. Here, we identify two bacterial protein families of noncanonical fatty acid biosynthesis starter enzymes and trans-acting polyketide enoyl reductases (ERs) as potential ancestors of scaffolding regions in fFAS. The architectures of both protein families are revealed by representative crystal structures of the starter enzyme FabY and DfnA-ER. In both families, a striking structural conservation of insertions to scaffolding elements in fFAS is observed, despite marginal sequence identity. The combined phylogenetic and structural data provide insights into the evolutionary origins of the complex multienzyme architecture of fFAS.
Evolutionary origins of the multienzyme architecture of giant fungal Fatty Acid synthase.,Bukhari HS, Jakob RP, Maier T Structure. 2014 Dec 2;22(12):1775-85. doi: 10.1016/j.str.2014.09.016. Epub 2014, Nov 13. PMID:25456814[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yuan Y, Sachdeva M, Leeds JA, Meredith TC. Fatty acid biosynthesis in Pseudomonas aeruginosa is initiated by the FabY class of beta-ketoacyl acyl carrier protein synthases. J Bacteriol. 2012 Oct;194(19):5171-84. doi: 10.1128/JB.00792-12. Epub 2012 Jun, 29. PMID:22753059 doi:http://dx.doi.org/10.1128/JB.00792-12
- ↑ Six DA, Yuan Y, Leeds JA, Meredith TC. Deletion of the beta-acetoacetyl synthase FabY in Pseudomonas aeruginosa induces hypoacylation of lipopolysaccharide and increases antimicrobial susceptibility. Antimicrob Agents Chemother. 2014;58(1):153-61. doi: 10.1128/AAC.01804-13. Epub, 2013 Oct 21. PMID:24145528 doi:http://dx.doi.org/10.1128/AAC.01804-13
- ↑ Bukhari HS, Jakob RP, Maier T. Evolutionary origins of the multienzyme architecture of giant fungal Fatty Acid synthase. Structure. 2014 Dec 2;22(12):1775-85. doi: 10.1016/j.str.2014.09.016. Epub 2014, Nov 13. PMID:25456814 doi:http://dx.doi.org/10.1016/j.str.2014.09.016
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