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| | <StructureSection load='3wef' size='340' side='right'caption='[[3wef]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='3wef' size='340' side='right'caption='[[3wef]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wef]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wef]] is a 6 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=3WEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPS:S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]+TRIHYDROGEN+THIODIPHOSPHATE'>FPS</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vj8|3vj8]], [[3vj9|3vj9]], [[3vja|3vja]], [[3vjb|3vjb]], [[3vjc|3vjc]], [[3vjd|3vjd]], [[3weg|3weg]], [[3weh|3weh]], [[3wei|3wei]], [[3wej|3wej]], [[3wek|3wek]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPS:S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]+TRIHYDROGEN+THIODIPHOSPHATE'>FPS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FDFT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Squalene_synthase Squalene synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.21 2.5.1.21] </span></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=3wef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wef OCA], [https://pdbe.org/3wef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wef RCSB], [https://www.ebi.ac.uk/pdbsum/3wef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wef ProSAT]</span></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=3wef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wef OCA], [https://pdbe.org/3wef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wef RCSB], [https://www.ebi.ac.uk/pdbsum/3wef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wef ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FDFT_HUMAN FDFT_HUMAN] |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Squalene synthase]]
| + | [[Category: Jeng WY]] |
| - | [[Category: Jeng, W Y]] | + | [[Category: Liu CI]] |
| - | [[Category: Liu, C I]] | + | [[Category: Wang AHJ]] |
| - | [[Category: Wang, A H.J]] | + | |
| - | [[Category: Cholesterol biosynthesis]]
| + | |
| - | [[Category: Farnesyl-diphosphate farnesyltransferase]]
| + | |
| - | [[Category: Head-to-head synthase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
FDFT_HUMAN
Publication Abstract from PubMed
Squalene synthase (SQS) is a divalent metal-ion-dependent enzyme that catalyzes the two-step reductive `head-to-head' condensation of two molecules of farnesyl pyrophosphate to form squalene using presqualene diphosphate (PSPP) as an intermediate. In this paper, the structures of human SQS and its mutants in complex with several substrate analogues and intermediates coordinated with Mg2+ or Mn2+ are presented, which stepwise delineate the biosynthetic pathway. Extensive study of the SQS active site has identified several critical residues that are involved in binding reduced nicotinamide dinucleotide phosphate (NADPH). Based on mutagenesis data and a locally closed (JK loop-in) structure observed in the hSQS-(F288L)-PSPP complex, an NADPH-binding model is proposed for SQS. The results identified four major steps (substrate binding, condensation, intermediate formation and translocation) of the ordered sequential mechanisms involved in the `1'-1' isoprenoid biosynthetic pathway. These new findings clarify previous hypotheses based on site-directed mutagenesis and biochemical analysis.
Structural insights into the catalytic mechanism of human squalene synthase.,Liu CI, Jeng WY, Chang WJ, Shih MF, Ko TP, Wang AH Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):231-41. doi:, 10.1107/S1399004713026230. Epub 2014 Jan 17. PMID:24531458[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu CI, Jeng WY, Chang WJ, Shih MF, Ko TP, Wang AH. Structural insights into the catalytic mechanism of human squalene synthase. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):231-41. doi:, 10.1107/S1399004713026230. Epub 2014 Jan 17. PMID:24531458 doi:http://dx.doi.org/10.1107/S1399004713026230
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