4cw5: Difference between revisions
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New page: '''Unreleased structure''' The entry 4cw5 is ON HOLD until Paper Publication Authors: Jakob, R.P., Buhkari, S.H.T., Maier, T. Description: A protein structure |
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==Crystal structure of the enoyl reductase domain of DfnA from Bacillus amyloliquefaciens== | |||
<StructureSection load='4cw5' size='340' side='right'caption='[[4cw5]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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='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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A7Z6E3_BACVZ A7Z6E3_BACVZ] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:25456814</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4cw5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus velezensis FZB42]] | |||
[[Category: Large Structures]] | |||
[[Category: Buhkari HST]] | |||
[[Category: Jakob RP]] | |||
[[Category: Maier T]] | |||
Latest revision as of 12:17, 20 December 2023
Crystal structure of the enoyl reductase domain of DfnA from Bacillus amyloliquefaciens
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