8ron
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human FAD synthase, isoform 2== | |
| + | <StructureSection load='8ron' size='340' side='right'caption='[[8ron]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ron]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RON 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]] 2.6Å</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=8ron FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ron OCA], [https://pdbe.org/8ron PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ron RCSB], [https://www.ebi.ac.uk/pdbsum/8ron PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ron ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/FAD1_HUMAN FAD1_HUMAN] Multiple acyl-CoA dehydrogenase deficiency, severe neonatal type;Multiple acyl-CoA dehydrogenase deficiency, mild type. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAD1_HUMAN FAD1_HUMAN] Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.<ref>PMID:16643857</ref> <ref>PMID:27259049</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human flavin adenine dinucleotide synthase (hFADS) is a bifunctional, multi-domain enzyme that exhibits both flavin mononucleotide adenylyltransferase and pyrophosphatase activities. Here we report the crystal structure of full-length hFADS2 and its C-terminal PAPS domain in complex with flavin adenine dinucleotide (FAD), and dissect the structural determinants underlying the contribution of each individual domain, within isoforms 1 and 2, to each of the two enzymatic activities. Structural and functional characterization performed on complete or truncated constructs confirmed that the C-terminal domain tightly binds FAD and catalyzes its synthesis, while the combination of the N-terminal molybdopterin-binding and KH domains is the minimal essential substructure required for the hydrolysis of FAD and other ADP-containing dinucleotides. hFADS2 associates in a stable C2-symmetric dimer, in which the packing of the KH domain of one protomer against the N-terminal domain of the other creates the adenosine-specific active site responsible for the hydrolytic activity. | ||
| - | + | Structural insights into the bifunctional enzyme human FAD synthase.,Leo G, Leone P, Ataie Kachoie E, Tolomeo M, Galluccio M, Indiveri C, Barile M, Capaldi S Structure. 2024 Jul 11;32(7):953-965.e5. doi: 10.1016/j.str.2024.04.006. Epub , 2024 Apr 29. PMID:38688286<ref>PMID:38688286</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8ron" style="background-color:#fffaf0;"></div> |
| - | [[Category: Capaldi | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Capaldi S]] | ||
| + | [[Category: Leo G]] | ||
Current revision
Crystal structure of human FAD synthase, isoform 2
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