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4uy5

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Revision as of 08:09, 5 August 2016

Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis

Structural highlights

4uy5 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	4uy6, 4uy7, 4uz0
Activity:	L-histidine N(alpha)-methyltransferase, with EC number 2.1.1.44
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

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

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/4uy5"

Categories: Jeong, J H | Kim, Y G | Antioxidant | S-adenosyl-l-methionine | Transferase

@@ Line 1: / Line 1: @@
 ==Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis==
 <StructureSection load='4uy5' size='340' side='right' caption='[[4uy5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <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://www.rcsb.org/pdb/explore.do?structureId=4uy5 RCSB], [http://www.ebi.ac.uk/pdbsum/4uy5 PDBsum]</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>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4uy5" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4uy5

From Proteopedia

Revision as of 08:09, 5 August 2016

Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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