5hxt: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase (D71M, E75A and H103Y Mutants) Complexed with IPP and DMSPP==
-<StructureSection load='5hxt' size='340' side='right' caption='[[5hxt]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+<StructureSection load='5hxt' size='340' side='right'caption='[[5hxt]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hxt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HXT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hxt]] is a 2 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=5HXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HXT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=IPR:ISOPENTYL+PYROPHOSPHATE'>IPR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=O4B:1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE'>O4B</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]] 2.15&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hxn|5hxn]], [[5hxo|5hxo]], [[5hxp|5hxp]], [[5hxq|5hxq]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=IPR:ISOPENTYL+PYROPHOSPHATE'>IPR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=O4B:1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE'>O4B</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5hxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxt OCA], [https://pdbe.org/5hxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hxt RCSB], [https://www.ebi.ac.uk/pdbsum/5hxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxt ProSAT]</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=5hxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxt OCA], [http://pdbe.org/5hxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hxt RCSB], [http://www.ebi.ac.uk/pdbsum/5hxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxt 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 5hxt" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Chan, Y T]]
+[[Category: Large Structures]]
-[[Category: Lee, C C]]
+[[Category: Solanum habrochaites]]
-[[Category: Wang, A H.J]]
+[[Category: Chan YT]]
-[[Category: Prenyltransferase]]
+[[Category: Lee CC]]
-[[Category: Transferase]]
+[[Category: Wang AHJ]]