6dii: Difference between revisions

Revision as of 06:33, 27 March 2019

Structure of Arabidopsis Fatty Acid Amide Hydrolase in Complex with methyl linolenyl fluorophosphonate

Structural highlights

6dii is a 12 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	GJY
Related:	6dhv
Activity:	Fatty acid amide hydrolase, with EC number 3.5.1.99
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FAAH_ARATH] Degrades bioactive fatty acid amides to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Converts N-actylethanolamine (NAE) to ethanolamine. Can also use oleamide or 2-arachidonylglycerol as substrates, but not indole-3-acetamide, 1-naphtalene-acetamide, nicotinic acid amide or L-asparagine. Might be involved in abscisic acid signaling and plant defense through distinctly different mechanisms not involving the catalytic activity.^[1] ^[2] ^[3] ^[4]

References

↑ Shrestha R, Dixon RA, Chapman KD. Molecular identification of a functional homologue of the mammalian fatty acid amide hydrolase in Arabidopsis thaliana. J Biol Chem. 2003 Sep 12;278(37):34990-7. Epub 2003 Jun 24. PMID:12824167 doi:https://dx.doi.org/10.1074/jbc.M305613200
↑ Wang YS, Shrestha R, Kilaru A, Wiant W, Venables BJ, Chapman KD, Blancaflor EB. Manipulation of Arabidopsis fatty acid amide hydrolase expression modifies plant growth and sensitivity to N-acylethanolamines. Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):12197-202. doi:, 10.1073/pnas.0603571103. Epub 2006 Jul 31. PMID:16880402 doi:https://dx.doi.org/10.1073/pnas.0603571103
↑ Kang L, Wang YS, Uppalapati SR, Wang K, Tang Y, Vadapalli V, Venables BJ, Chapman KD, Blancaflor EB, Mysore KS. Overexpression of a fatty acid amide hydrolase compromises innate immunity in Arabidopsis. Plant J. 2008 Oct;56(2):336-349. doi: 10.1111/j.1365-313X.2008.03603.x. Epub 2008, Jul 4. PMID:18643971 doi:https://dx.doi.org/10.1111/j.1365-313X.2008.03603.x
↑ Kim SC, Kang L, Nagaraj S, Blancaflor EB, Mysore KS, Chapman KD. Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic activity influences growth but not sensitivity to abscisic acid or pathogens. J Biol Chem. 2009 Dec 4;284(49):34065-74. doi: 10.1074/jbc.M109.059022. Epub 2009, Sep 30. PMID:19801664 doi:https://dx.doi.org/10.1074/jbc.M109.059022

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OCA

[1] Shrestha R, Dixon RA, Chapman KD. Molecular identification of a functional homologue of the mammalian fatty acid amide hydrolase in Arabidopsis thaliana. J Biol Chem. 2003 Sep 12;278(37):34990-7. Epub 2003 Jun 24. PMID:12824167 doi:https://dx.doi.org/10.1074/jbc.M305613200

[2] Wang YS, Shrestha R, Kilaru A, Wiant W, Venables BJ, Chapman KD, Blancaflor EB. Manipulation of Arabidopsis fatty acid amide hydrolase expression modifies plant growth and sensitivity to N-acylethanolamines. Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):12197-202. doi:, 10.1073/pnas.0603571103. Epub 2006 Jul 31. PMID:16880402 doi:https://dx.doi.org/10.1073/pnas.0603571103

[3] Kang L, Wang YS, Uppalapati SR, Wang K, Tang Y, Vadapalli V, Venables BJ, Chapman KD, Blancaflor EB, Mysore KS. Overexpression of a fatty acid amide hydrolase compromises innate immunity in Arabidopsis. Plant J. 2008 Oct;56(2):336-349. doi: 10.1111/j.1365-313X.2008.03603.x. Epub 2008, Jul 4. PMID:18643971 doi:https://dx.doi.org/10.1111/j.1365-313X.2008.03603.x

[4] Kim SC, Kang L, Nagaraj S, Blancaflor EB, Mysore KS, Chapman KD. Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic activity influences growth but not sensitivity to abscisic acid or pathogens. J Biol Chem. 2009 Dec 4;284(49):34065-74. doi: 10.1074/jbc.M109.059022. Epub 2009, Sep 30. PMID:19801664 doi:https://dx.doi.org/10.1074/jbc.M109.059022

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6dii is ON HOLD  until Paper Publication
+==Structure of Arabidopsis Fatty Acid Amide Hydrolase in Complex with methyl linolenyl fluorophosphonate==
+<StructureSection load='6dii' size='340' side='right'caption='[[6dii]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-Authors: Aziz, M., Wang, X., Tripathi, A., Bankaitis, V., Chapman, K.D.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6dii]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DII FirstGlance]. <br>
-Description: Structure of Arabidopsis Fatty Acid Amide Hydrolase in Complex with methyl linolenyl fluorophosphonate
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GJY:methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate'>GJY</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6dhv|6dhv]]</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fatty_acid_amide_hydrolase Fatty acid amide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.99 3.5.1.99] </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=6dii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dii OCA], [http://pdbe.org/6dii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dii RCSB], [http://www.ebi.ac.uk/pdbsum/6dii PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dii ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FAAH_ARATH FAAH_ARATH]] Degrades bioactive fatty acid amides to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Converts N-actylethanolamine (NAE) to ethanolamine. Can also use oleamide or 2-arachidonylglycerol as substrates, but not indole-3-acetamide, 1-naphtalene-acetamide, nicotinic acid amide or L-asparagine. Might be involved in abscisic acid signaling and plant defense through distinctly different mechanisms not involving the catalytic activity.<ref>PMID:12824167</ref> <ref>PMID:16880402</ref> <ref>PMID:18643971</ref> <ref>PMID:19801664</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Fatty acid amide hydrolase]]
+[[Category: Large Structures]]
+[[Category: Aziz, M]]
 [[Category: Bankaitis, V]]
+[[Category: Chapman, K D]]
 [[Category: Tripathi, A]]
-[[Category: Chapman, K.D]]
 [[Category: Wang, X]]
-[[Category: Aziz, M]]
+[[Category: Faah]]
+[[Category: Hydrolase]]
+[[Category: Nae signaling]]

6dii: Difference between revisions

Revision as of 06:33, 27 March 2019

Structure of Arabidopsis Fatty Acid Amide Hydrolase in Complex with methyl linolenyl fluorophosphonate

Structural highlights

Function

References

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