5hk8: Difference between revisions

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<StructureSection load='5hk8' size='340' side='right'caption='[[5hk8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='5hk8' size='340' side='right'caption='[[5hk8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5hk8]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HK8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HK8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5hk8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HK8 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPD, MES16, At4g16690, dl4370c, FCAALL.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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]] 2.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pheophorbidase Pheophorbidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.82 3.1.1.82] </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=5hk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk8 OCA], [https://pdbe.org/5hk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hk8 RCSB], [https://www.ebi.ac.uk/pdbsum/5hk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk8 OCA], [http://pdbe.org/5hk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hk8 RCSB], [http://www.ebi.ac.uk/pdbsum/5hk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PPD_ARATH PPD_ARATH]] Involved in the chlorophyll breakdown by its action in fluorescent chlorophyll catabolites (FCCs) demethylation. Demethylates the C13(2)-carboxymethyl group present at the isocyclic ring of chlorophyll. Also able to catalyze pheophorbides in vitro. Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro.<ref>PMID:18467465</ref> <ref>PMID:22147518</ref>
[https://www.uniprot.org/uniprot/MES16_ARATH MES16_ARATH] Involved in the chlorophyll breakdown by its action in fluorescent chlorophyll catabolites (FCCs) demethylation (PubMed:22147518, PubMed:23723324, PubMed:24302623). Demethylates the C13(2)-carboxymethyl group present at the isocyclic ring of chlorophyll (PubMed:22147518). Uses primary fluorescent dioxobilin-type chlorophyll catabolite (pFDCC) as substrate to produce O13(4)-desmethyl pFDCC (PubMed:23723324, PubMed:24302623). Also able to catalyze pheophorbides in vitro (PubMed:22147518). Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro (PubMed:18467465, PubMed:27109476).<ref>PMID:18467465</ref> <ref>PMID:22147518</ref> <ref>PMID:23723324</ref> <ref>PMID:24302623</ref> <ref>PMID:27109476</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pheophorbidase]]
[[Category: Li H]]
[[Category: Li, H]]
[[Category: Pu H]]
[[Category: Pu, H]]
[[Category: Hydrolase]]
[[Category: Hydrolase superfamily]]
[[Category: Mes16]]
[[Category: Methylesterase protein]]

Latest revision as of 10:39, 9 August 2023

Crystal structure of a methylesterase protein MES16 from ArabidopsisCrystal structure of a methylesterase protein MES16 from Arabidopsis

Structural highlights

5hk8 is a 6 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MES16_ARATH Involved in the chlorophyll breakdown by its action in fluorescent chlorophyll catabolites (FCCs) demethylation (PubMed:22147518, PubMed:23723324, PubMed:24302623). Demethylates the C13(2)-carboxymethyl group present at the isocyclic ring of chlorophyll (PubMed:22147518). Uses primary fluorescent dioxobilin-type chlorophyll catabolite (pFDCC) as substrate to produce O13(4)-desmethyl pFDCC (PubMed:23723324, PubMed:24302623). Also able to catalyze pheophorbides in vitro (PubMed:22147518). Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro (PubMed:18467465, PubMed:27109476).[1] [2] [3] [4] [5]

References

  1. ↑ Yang Y, Xu R, Ma CJ, Vlot AC, Klessig DF, Pichersky E. Inactive methyl indole-3-acetic acid ester can be hydrolyzed and activated by several esterases belonging to the AtMES esterase family of Arabidopsis. Plant Physiol. 2008 Jul;147(3):1034-45. doi: 10.1104/pp.108.118224. Epub 2008 May, 8. PMID:18467465 doi:http://dx.doi.org/10.1104/pp.108.118224
  2. ↑ Christ B, Schelbert S, Aubry S, Sussenbacher I, Muller T, Krautler B, Hortensteiner S. MES16, a member of the methylesterase protein family, specifically demethylates fluorescent chlorophyll catabolites during chlorophyll breakdown in Arabidopsis. Plant Physiol. 2012 Feb;158(2):628-41. doi: 10.1104/pp.111.188870. Epub 2011 Dec , 6. PMID:22147518 doi:http://dx.doi.org/10.1104/pp.111.188870
  3. ↑ Christ B, Süssenbacher I, Moser S, Bichsel N, Egert A, Müller T, Kräutler B, Hörtensteiner S. Cytochrome P450 CYP89A9 is involved in the formation of major chlorophyll catabolites during leaf senescence in Arabidopsis. Plant Cell. 2013 May;25(5):1868-80. PMID:23723324 doi:10.1105/tpc.113.112151
  4. ↑ Süssenbacher I, Christ B, Hörtensteiner S, Kräutler B. Hydroxymethylated phyllobilins: a puzzling new feature of the dioxobilin branch of chlorophyll breakdown. Chemistry. 2014 Jan 3;20(1):87-92. PMID:24302623 doi:10.1002/chem.201303398
  5. ↑ Li H, Pu H. Crystal structure of methylesterase family member 16 (MES16) from Arabidopsis thaliana. Biochem Biophys Res Commun. 2016 May 20;474(1):226-231. PMID:27109476 doi:10.1016/j.bbrc.2016.04.115

5hk8, resolution 2.80Å

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