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| | <StructureSection load='5hxo' size='340' side='right'caption='[[5hxo]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='5hxo' size='340' side='right'caption='[[5hxo]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hxo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lycopersicon_habrochaites Lycopersicon habrochaites]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HXO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hxo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_habrochaites Solanum habrochaites]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HXO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hxn|5hxn]], [[5hxp|5hxp]], [[5hxq|5hxq]], [[5hxt|5hxt]]</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]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZFPS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=62890 Lycopersicon habrochaites])</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=5hxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxo OCA], [https://pdbe.org/5hxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hxo RCSB], [https://www.ebi.ac.uk/pdbsum/5hxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxo ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(2Z,6Z)-farnesyl_diphosphate_synthase (2Z,6Z)-farnesyl diphosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.92 2.5.1.92] </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=5hxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxo OCA], [http://pdbe.org/5hxo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hxo RCSB], [http://www.ebi.ac.uk/pdbsum/5hxo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ZFPS_SOLHA ZFPS_SOLHA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lycopersicon habrochaites]] | + | [[Category: Solanum habrochaites]] |
| - | [[Category: Chan, Y T]] | + | [[Category: Chan YT]] |
| - | [[Category: Lee, C C]] | + | [[Category: Lee CC]] |
| - | [[Category: Wang, A H.J]] | + | [[Category: Wang AHJ]] |
| - | [[Category: Prenyltransferase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
ZFPS_SOLHA
Publication Abstract from PubMed
Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. Z,Z-Farnesyl diphosphate (Z,Z-FPP), synthesized by Z,Z-farnesyl diphosphate synthase (zFPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated zFPS (DeltazFPS) was determined. Irregular products including lavandulyl diphosphate and an unknown compound were surprisingly found. Apart from the truncated N-terminus as a functional regulator, structure-based analysis and mutagenesis assays revealed a residue H103 in DeltazFPS as one of the key elements to this irregular function. A series of substrate-enzyme complex structures were obtained from DeltazFPS-H103Y by co-crystallizing with isopentenyl diphosphate, dimethylallyl thiolodiphosphate, or both. Various substrate-binding modes were revealed. The catalytic mechanisms of both the head-to-tail and head-to-middle reactions in DeltazFPS were proposed. Functional switch between the two mechanisms in this enzyme and the essential role played by the flexible C-terminus were elucidated as well.
Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase.,Chan YT, Ko TP, Yao SH, Chen YW, Lee CC, Wang AH ACS Omega. 2017 Mar 31;2(3):930-936. doi: 10.1021/acsomega.6b00562. Epub 2017 Mar, 16. PMID:30023621[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chan YT, Ko TP, Yao SH, Chen YW, Lee CC, Wang AH. Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase. ACS Omega. 2017 Mar 31;2(3):930-936. doi: 10.1021/acsomega.6b00562. Epub 2017 Mar, 16. PMID:30023621 doi:http://dx.doi.org/10.1021/acsomega.6b00562
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