View source for 5hxo


==Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase with D71M, E75A and H103Y Mutants==
<StructureSection load='5hxo' size='340' side='right'caption='[[5hxo]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ZFPS_SOLHA ZFPS_SOLHA] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:30023621</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hxo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solanum habrochaites]]
[[Category: Chan YT]]
[[Category: Lee CC]]
[[Category: Wang AHJ]]