6riw
From Proteopedia
(Difference between revisions)
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==PfaC Keto synthase-Chain length factor== | ==PfaC Keto synthase-Chain length factor== | ||
| - | <StructureSection load='6riw' size='340' side='right'caption='[[6riw]]' scene=''> | + | <StructureSection load='6riw' size='340' side='right'caption='[[6riw]], [[Resolution|resolution]] 1.85Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIW OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6riw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moritella_marina Moritella marina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RIW FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6riw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6riw OCA], [https://pdbe.org/6riw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6riw RCSB], [https://www.ebi.ac.uk/pdbsum/6riw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6riw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9RA19_MORMI Q9RA19_MORMI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Long-chain polyunsaturated fatty acids (LC-PUFAs) are essential ingredients of the human diet. They are synthesized by LC-PUFA synthases (PFASs) expressed in marine bacteria and other organisms. PFASs are large enzyme complexes that are homologous to mammalian fatty acid synthases and microbial polyketide synthases. One subunit of each PFAS harbors consecutive ketosynthase (KSc) and chain length factor (CLF) domains that collectively catalyze the elongation of a nascent fatty acyl chain via iterative carbon-carbon bond formation. We report the X-ray crystal structure of the KS-CLF didomain from a well-studied PFAS in Moritella marina. Our structure, in combination with biochemical analysis, provides a foundation for understanding the mechanism of substrate recognition and chain length control by the KS-CLF didomain as well as its interaction with a cognate acyl carrier protein partner. | ||
| + | |||
| + | Structure and Mechanism of the Ketosynthase-Chain Length Factor Didomain from a Prototypical Polyunsaturated Fatty Acid Synthase.,Santin O, Yuet K, Khosla C, Moncalian G Biochemistry. 2020 Dec 22;59(50):4735-4743. doi: 10.1021/acs.biochem.0c00785. , Epub 2020 Dec 7. PMID:33283513<ref>PMID:33283513</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6riw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Moritella marina]] | ||
[[Category: Moncalian G]] | [[Category: Moncalian G]] | ||
[[Category: Santin O]] | [[Category: Santin O]] | ||
Current revision
PfaC Keto synthase-Chain length factor
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