4pip

From Proteopedia

(Difference between revisions)

Revision as of 13:07, 1 February 2023

Engineered EgtD variant EgtD-M252V,E282A in complex with tryptophan and SAH

Structural highlights

4pip is a 4 chain structure with sequence from Mycolicibacterium smegmatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EGTD_MYCS2 Catalyzes the methylations of histidine to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine). Histidine and alpha-N,N-dimethylhistidine are preferred substrates.^[1]

Publication Abstract from PubMed

Ergothioneine is an N-alpha-trimethyl-2-thiohistidine derivative that occurs in human, plant, fungal, and bacterial cells. Biosynthesis of this redox-active betaine starts with trimethylation of the alpha-amino group of histidine. The three consecutive methyl transfers are catalyzed by the S-adenosylmethionine-dependent methyltransferase EgtD. Three crystal structures of this enzyme in the absence and in the presence of N-alpha-dimethylhistidine and S-adenosylhomocysteine implicate a preorganized array of hydrophilic interactions as the determinants for substrate specificity and apparent processivity. We identified two active site mutations that change the substrate specificity of EgtD 107 -fold and transform the histidine-methyltransferase into a proficient tryptophan-methyltransferase. Finally, a genomic search for EgtD homologues in fungal genomes revealed tyrosine and tryptophan trimethylation activity as a frequent trait in ascomycetous and basidomycetous fungi.

Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis.,Vit A, Misson L, Blankenfeldt W, Seebeck FP Chembiochem. 2014 Nov 17. doi: 10.1002/cbic.201402522. PMID:25404173^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Seebeck FP. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. J Am Chem Soc. 2010 May 19;132(19):6632-3. doi: 10.1021/ja101721e. PMID:20420449 doi:http://dx.doi.org/10.1021/ja101721e
↑ Vit A, Misson L, Blankenfeldt W, Seebeck FP. Ergothioneine Biosynthetic Methyltransferase EgtD Reveals the Structural Basis of Aromatic Amino Acid Betaine Biosynthesis. Chembiochem. 2014 Nov 17. doi: 10.1002/cbic.201402522. PMID:25404173 doi:http://dx.doi.org/10.1002/cbic.201402522

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4pip"

Categories: Large Structures | Mycolicibacterium smegmatis | Blankenfeldt W | Seebeck FP | Vit A

@@ Line 1: / Line 1: @@
 ==Engineered EgtD variant EgtD-M252V,E282A in complex with tryptophan and SAH==
-<StructureSection load='4pip' size='340' side='right' caption='[[4pip]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='4pip' size='340' side='right'caption='[[4pip]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4pip]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_smegmatis"_trevisan_1889 "bacillus smegmatis" trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PIP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4pip]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PIP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pim|4pim]], [[4pin|4pin]], [[4pio|4pio]]</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=4pip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pip OCA], [https://pdbe.org/4pip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pip RCSB], [https://www.ebi.ac.uk/pdbsum/4pip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pip ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">egtD, MSMEG_6247, MSMEI_6086 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1772 "Bacillus smegmatis" Trevisan 1889])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-histidine_N(alpha)-methyltransferase L-histidine N(alpha)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.44 2.1.1.44] </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=4pip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pip OCA], [http://pdbe.org/4pip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pip RCSB], [http://www.ebi.ac.uk/pdbsum/4pip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pip ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EGTD_MYCS2 EGTD_MYCS2]] Catalyzes the methylations of histidine to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine). Histidine and alpha-N,N-dimethylhistidine are preferred substrates.<ref>PMID:20420449</ref>
+[https://www.uniprot.org/uniprot/EGTD_MYCS2 EGTD_MYCS2] Catalyzes the methylations of histidine to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine). Histidine and alpha-N,N-dimethylhistidine are preferred substrates.<ref>PMID:20420449</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus smegmatis trevisan 1889]]
+[[Category: Large Structures]]
-[[Category: Blankenfeldt, W]]
+[[Category: Mycolicibacterium smegmatis]]
-[[Category: Seebeck, F P]]
+[[Category: Blankenfeldt W]]
-[[Category: Vit, A]]
+[[Category: Seebeck FP]]
-[[Category: Ergothioneine]]
+[[Category: Vit A]]
-[[Category: Histidine betaine]]
-[[Category: Methyltransferase]]
-[[Category: Transferase]]

4pip

From Proteopedia

Revision as of 13:07, 1 February 2023

Engineered EgtD variant EgtD-M252V,E282A in complex with tryptophan and SAH

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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