5hxo

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==Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase with D71M, E75A and H103Y Mutants==
==Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase with D71M, E75A and H103Y Mutants==
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<StructureSection load='5hxo' size='340' side='right' caption='[[5hxo]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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<StructureSection load='5hxo' size='340' side='right'caption='[[5hxo]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hxo]] is a 1 chain structure. 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>
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<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>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hxn|5hxn]], [[5hxp|5hxp]], [[5hxq|5hxq]], [[5hxt|5hxt]]</td></tr>
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<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='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='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>
<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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hxo" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
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[[Category: Lycopersicon habrochaites]]
[[Category: Chan, Y T]]
[[Category: Chan, Y T]]
[[Category: Lee, C C]]
[[Category: Lee, C C]]

Revision as of 08:50, 18 December 2019

Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase with D71M, E75A and H103Y Mutants

PDB ID 5hxo

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