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| | <StructureSection load='4cw5' size='340' side='right'caption='[[4cw5]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4cw5' size='340' side='right'caption='[[4cw5]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cw5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacvz Bacvz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CW5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cw5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_velezensis_FZB42 Bacillus velezensis FZB42]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CW5 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></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]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cw4|4cw4]]</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=4cw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cw5 OCA], [https://pdbe.org/4cw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cw5 RCSB], [https://www.ebi.ac.uk/pdbsum/4cw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cw5 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=4cw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cw5 OCA], [http://pdbe.org/4cw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cw5 RCSB], [http://www.ebi.ac.uk/pdbsum/4cw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cw5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A7Z6E3_BACVZ A7Z6E3_BACVZ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacvz]] | + | [[Category: Bacillus velezensis FZB42]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buhkari, H S.T]] | + | [[Category: Buhkari HST]] |
| - | [[Category: Jakob, R P]] | + | [[Category: Jakob RP]] |
| - | [[Category: Maier, T]] | + | [[Category: Maier T]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Polyketide]]
| + | |
| - | [[Category: Trans-at pk]]
| + | |
| Structural highlights
Function
A7Z6E3_BACVZ
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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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