7wh9: Difference between revisions

Revision as of 07:35, 11 January 2023

holo structure of emodin 1-OH O-methyltransferase complex with emodin and S-Adenosyl-L-homocysteine

Structural highlights

7wh9 is a 3 chain structure with sequence from Aspergillus terreus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	EMO, SAH
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GEDA_ASPTN O-methyltransferase; part of the gene cluster that mediates the biosynthesis of geodin, an intermediate in the biosynthesis of other natural products (PubMed:7665560, PubMed:19549600, PubMed:24009710). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) gedC (PubMed:12536215, PubMed:19549600). The atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC (PubMed:19549600). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodinanthrone (PubMed:24009710). The next step is performed by the emodinanthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin (PubMed:1810248). Emodin O-methyltransferase encoded probably by gedA then catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:1444712). Ring cleavage of questin by questin oxidase gedK leads to desmethylsulochrin via several intermediates including questin epoxide (PubMed:3182756). Another methylation step probably catalyzed by methyltransferase gedG leads to the formation of sulochrin which is further converted to dihydrogeodin by the sulochrin halogenase gedL (PubMed:24009710). Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol oxidative coupling reaction converting dihydrogeodin to geodin (PubMed:7665560).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

References

↑ Askenazi M, Driggers EM, Holtzman DA, Norman TC, Iverson S, Zimmer DP, Boers ME, Blomquist PR, Martinez EJ, Monreal AW, Feibelman TP, Mayorga ME, Maxon ME, Sykes K, Tobin JV, Cordero E, Salama SR, Trueheart J, Royer JC, Madden KT. Integrating transcriptional and metabolite profiles to direct the engineering of lovastatin-producing fungal strains. Nat Biotechnol. 2003 Feb;21(2):150-6. doi: 10.1038/nbt781. Epub 2003 Jan 21. PMID:12536215 doi:https://dx.doi.org/10.1038/nbt781
↑ Chen ZG, Fujii I, Ebizuka Y, Sankawa U. Emodin O-methyltransferase from Aspergillus terreus. Arch Microbiol. 1992;158(1):29-34. doi: 10.1007/BF00249062. PMID:1444712 doi:https://dx.doi.org/10.1007/BF00249062
↑ Fujii I, Chen ZG, Ebizuka Y, Sankawa U. Identification of emodinanthrone oxygenase in fungus Aspergillus terreus. Biochem Int. 1991 Dec;25(6):1043-9. PMID:1810248
↑ Awakawa T, Yokota K, Funa N, Doi F, Mori N, Watanabe H, Horinouchi S. Physically discrete beta-lactamase-type thioesterase catalyzes product release in atrochrysone synthesis by iterative type I polyketide synthase. Chem Biol. 2009 Jun 26;16(6):613-23. doi: 10.1016/j.chembiol.2009.04.004. PMID:19549600 doi:https://dx.doi.org/10.1016/j.chembiol.2009.04.004
↑ Nielsen MT, Nielsen JB, Anyaogu DC, Holm DK, Nielsen KF, Larsen TO, Mortensen UH. Heterologous reconstitution of the intact geodin gene cluster in Aspergillus nidulans through a simple and versatile PCR based approach. PLoS One. 2013 Aug 23;8(8):e72871. doi: 10.1371/journal.pone.0072871. eCollection , 2013. PMID:24009710 doi:https://dx.doi.org/10.1371/journal.pone.0072871
↑ Fujii I, Ebizuka Y, Sankawa U. A novel anthraquinone ring cleavage enzyme from Aspergillus terreus. J Biochem. 1988 May;103(5):878-83. doi: 10.1093/oxfordjournals.jbchem.a122365. PMID:3182756 doi:https://dx.doi.org/10.1093/oxfordjournals.jbchem.a122365
↑ Huang KX, Fujii I, Ebizuka Y, Gomi K, Sankawa U. Molecular cloning and heterologous expression of the gene encoding dihydrogeodin oxidase, a multicopper blue enzyme from Aspergillus terreus. J Biol Chem. 1995 Sep 15;270(37):21495-502. doi: 10.1074/jbc.270.37.21495. PMID:7665560 doi:https://dx.doi.org/10.1074/jbc.270.37.21495

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Askenazi M, Driggers EM, Holtzman DA, Norman TC, Iverson S, Zimmer DP, Boers ME, Blomquist PR, Martinez EJ, Monreal AW, Feibelman TP, Mayorga ME, Maxon ME, Sykes K, Tobin JV, Cordero E, Salama SR, Trueheart J, Royer JC, Madden KT. Integrating transcriptional and metabolite profiles to direct the engineering of lovastatin-producing fungal strains. Nat Biotechnol. 2003 Feb;21(2):150-6. doi: 10.1038/nbt781. Epub 2003 Jan 21. PMID:12536215 doi:https://dx.doi.org/10.1038/nbt781

[2] Chen ZG, Fujii I, Ebizuka Y, Sankawa U. Emodin O-methyltransferase from Aspergillus terreus. Arch Microbiol. 1992;158(1):29-34. doi: 10.1007/BF00249062. PMID:1444712 doi:https://dx.doi.org/10.1007/BF00249062

[3] Fujii I, Chen ZG, Ebizuka Y, Sankawa U. Identification of emodinanthrone oxygenase in fungus Aspergillus terreus. Biochem Int. 1991 Dec;25(6):1043-9. PMID:1810248

[4] Awakawa T, Yokota K, Funa N, Doi F, Mori N, Watanabe H, Horinouchi S. Physically discrete beta-lactamase-type thioesterase catalyzes product release in atrochrysone synthesis by iterative type I polyketide synthase. Chem Biol. 2009 Jun 26;16(6):613-23. doi: 10.1016/j.chembiol.2009.04.004. PMID:19549600 doi:https://dx.doi.org/10.1016/j.chembiol.2009.04.004

[5] Nielsen MT, Nielsen JB, Anyaogu DC, Holm DK, Nielsen KF, Larsen TO, Mortensen UH. Heterologous reconstitution of the intact geodin gene cluster in Aspergillus nidulans through a simple and versatile PCR based approach. PLoS One. 2013 Aug 23;8(8):e72871. doi: 10.1371/journal.pone.0072871. eCollection , 2013. PMID:24009710 doi:https://dx.doi.org/10.1371/journal.pone.0072871

[6] Fujii I, Ebizuka Y, Sankawa U. A novel anthraquinone ring cleavage enzyme from Aspergillus terreus. J Biochem. 1988 May;103(5):878-83. doi: 10.1093/oxfordjournals.jbchem.a122365. PMID:3182756 doi:https://dx.doi.org/10.1093/oxfordjournals.jbchem.a122365

[7] Huang KX, Fujii I, Ebizuka Y, Gomi K, Sankawa U. Molecular cloning and heterologous expression of the gene encoding dihydrogeodin oxidase, a multicopper blue enzyme from Aspergillus terreus. J Biol Chem. 1995 Sep 15;270(37):21495-502. doi: 10.1074/jbc.270.37.21495. PMID:7665560 doi:https://dx.doi.org/10.1074/jbc.270.37.21495

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7wh9 is ON HOLD  until Paper Publication
+==holo structure of emodin 1-OH O-methyltransferase complex with emodin and S-Adenosyl-L-homocysteine==
+<StructureSection load='7wh9' size='340' side='right'caption='[[7wh9]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7wh9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus Aspergillus terreus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WH9 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMO:3-METHYL-1,6,8-TRIHYDROXYANTHRAQUINONE'>EMO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7wh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wh9 OCA], [https://pdbe.org/7wh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wh9 RCSB], [https://www.ebi.ac.uk/pdbsum/7wh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wh9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GEDA_ASPTN GEDA_ASPTN] O-methyltransferase; part of the gene cluster that mediates the biosynthesis of geodin, an intermediate in the biosynthesis of other natural products (PubMed:7665560, PubMed:19549600, PubMed:24009710). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) gedC (PubMed:12536215, PubMed:19549600). The atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC (PubMed:19549600). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodinanthrone (PubMed:24009710). The next step is performed by the emodinanthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin (PubMed:1810248). Emodin O-methyltransferase encoded probably by gedA then catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:1444712). Ring cleavage of questin by questin oxidase gedK leads to desmethylsulochrin via several intermediates including questin epoxide (PubMed:3182756). Another methylation step probably catalyzed by methyltransferase gedG leads to the formation of sulochrin which is further converted to dihydrogeodin by the sulochrin halogenase gedL (PubMed:24009710). Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol oxidative coupling reaction converting dihydrogeodin to geodin (PubMed:7665560).<ref>PMID:12536215</ref> <ref>PMID:1444712</ref> <ref>PMID:1810248</ref> <ref>PMID:19549600</ref> <ref>PMID:24009710</ref> <ref>PMID:3182756</ref> <ref>PMID:7665560</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aspergillus terreus]]
+[[Category: Large Structures]]
+[[Category: Liang YJ]]
+[[Category: Lu XF]]
+[[Category: Qi FF]]
+[[Category: Xue YY]]

7wh9: Difference between revisions

Revision as of 07:35, 11 January 2023

holo structure of emodin 1-OH O-methyltransferase complex with emodin and S-Adenosyl-L-homocysteine

Structural highlights

Function

References

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