|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis== | | ==Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis== |
| - | <StructureSection load='4uy5' size='340' side='right' caption='[[4uy5]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4uy5' size='340' side='right'caption='[[4uy5]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4uy5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UY5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uy5]] is a 1 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=4UY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UY5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4uy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy5 OCA], [https://pdbe.org/4uy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uy5 RCSB], [https://www.ebi.ac.uk/pdbsum/4uy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uy5 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uy6|4uy6]], [[4uy7|4uy7]], [[4uz0|4uz0]]</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=4uy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uy5 OCA], [http://pdbe.org/4uy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uy5 RCSB], [http://www.ebi.ac.uk/pdbsum/4uy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uy5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Jeong, J H]] | + | [[Category: Large Structures]] |
| - | [[Category: Kim, Y G]] | + | [[Category: Mycolicibacterium smegmatis]] |
| - | [[Category: Antioxidant]] | + | [[Category: Jeong JH]] |
| - | [[Category: S-adenosyl-l-methionine]] | + | [[Category: Kim YG]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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
EgtD is an S-adenosyl-l-methionine (SAM)-dependent histidine N,N,N-methyltransferase that catalyzes the formation of hercynine from histidine in the ergothioneine biosynthetic process of Mycobacterium smegmatis. Ergothioneine is a secreted antioxidant that protects mycobacterium from oxidative stress. Here, we present three crystal structures of EgtD in the apo form, the histidine-bound form, and the S-adenosyl-l-homocysteine (SAH)/histidine-bound form. The study revealed that EgtD consists of two distinct domains: a typical methyltransferase domain and a unique substrate binding domain. The histidine binding pocket of the substrate binding domain primarily recognizes the imidazole ring and carboxylate group of histidine rather than the amino group, explaining the high selectivity for histidine and/or (mono-, di-) methylated histidine as substrates. In addition, SAM binding to the MTase domain induced a conformational change in EgtD to facilitate the methyl transfer reaction. The structural analysis provides insights into the putative catalytic mechanism of EgtD in a processive trimethylation reaction.
Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis.,Jeong JH, Cha HJ, Ha SC, Rojviriya C, Kim YG Biochem Biophys Res Commun. 2014 Oct 3;452(4):1098-103. doi:, 10.1016/j.bbrc.2014.09.058. Epub 2014 Sep 22. PMID:25251321[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
- ↑ Jeong JH, Cha HJ, Ha SC, Rojviriya C, Kim YG. Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis. Biochem Biophys Res Commun. 2014 Oct 3;452(4):1098-103. doi:, 10.1016/j.bbrc.2014.09.058. Epub 2014 Sep 22. PMID:25251321 doi:http://dx.doi.org/10.1016/j.bbrc.2014.09.058
|
