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==MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 1==
==MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 1==
<StructureSection load='3ssm' size='340' side='right' caption='[[3ssm]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='3ssm' size='340' side='right'caption='[[3ssm]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ssm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'micromonospora_griseorubida' 'micromonospora griseorubida']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SSM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ssm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_griseorubida Micromonospora griseorubida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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]] 2.247&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ssn|3ssn]], [[3sso|3sso]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mycE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28040 'Micromonospora griseorubida'])</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=3ssm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssm OCA], [https://pdbe.org/3ssm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ssm RCSB], [https://www.ebi.ac.uk/pdbsum/3ssm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ssm ProSAT]</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=3ssm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ssm RCSB], [http://www.ebi.ac.uk/pdbsum/3ssm PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYCE_MICGR MYCE_MICGR]] O-methyltransferase that catalyzes the conversion of mycinamicin VI to mycinamicin III in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic.<ref>PMID:19415708</ref> <ref>PMID:21884704</ref> 
[https://www.uniprot.org/uniprot/MYCE_MICGR MYCE_MICGR] O-methyltransferase that catalyzes the conversion of mycinamicin VI to mycinamicin III in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic.<ref>PMID:19415708</ref> <ref>PMID:21884704</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
O-linked methylation of sugar substituents is a common modification in the biosynthesis of many natural products and is catalyzed by multiple families of S-adenosyl-L-methionine (SAM or AdoMet)-dependent methyltransferases (MTs). Mycinamicins, potent antibiotics from Micromonospora griseorubida, can be methylated at two positions on a 6-deoxyallose substituent. The first methylation is catalyzed by MycE, a SAM- and metal-dependent MT. Crystal structures were determined for MycE bound to the product S-adenosyl-L-homocysteine (AdoHcy) and magnesium, both with and without the natural substrate mycinamicin VI. This represents the first structure of a natural product sugar MT in complex with its natural substrate. MycE is a tetramer of a two-domain polypeptide, comprising a C-terminal catalytic MT domain and an N-terminal auxiliary domain, which is important for quaternary assembly and for substrate binding. The symmetric MycE tetramer has a novel MT organization in which each of the four active sites is formed at the junction of three monomers within the tetramer. The active-site structure supports a mechanism in which a conserved histidine acts as a general base, and the metal ion helps to position the methyl acceptor and to stabilize a hydroxylate intermediate. A conserved tyrosine is suggested to support activity through interactions with the transferred methyl group from the SAM methyl donor. The structure of the free enzyme reveals a dramatic order-disorder transition in the active site relative to the S-adenosyl-L-homocysteine complexes, suggesting a mechanism for product/substrate exchange through concerted movement of five loops and the polypeptide C-terminus.
 
A new structural form in the SAM/metal-dependent omethyltransferase family: MycE from the mycinamicin biosynthetic pathway.,Akey DL, Li S, Konwerski JR, Confer LA, Bernard SM, Anzai Y, Kato F, Sherman DH, Smith JL J Mol Biol. 2011 Oct 21;413(2):438-50. Epub 2011 Aug 23. PMID:21884704<ref>PMID:21884704</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Micromonospora griseorubida]]
[[Category: Micromonospora griseorubida]]
[[Category: Akey, D L]]
[[Category: Akey DL]]
[[Category: Smith, J L]]
[[Category: Smith JL]]
[[Category: Macrolide]]
[[Category: Methyltransferase]]
[[Category: Natural product]]
[[Category: Rossmann fold]]
[[Category: Transferase]]

Latest revision as of 12:56, 1 March 2024

MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 1MycE Methyltransferase from the Mycinamycin Biosynthetic Pathway in Complex with Mg and SAH, Crystal form 1

Structural highlights

3ssm is a 4 chain structure with sequence from Micromonospora griseorubida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.247Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYCE_MICGR O-methyltransferase that catalyzes the conversion of mycinamicin VI to mycinamicin III in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic.[1] [2]

See Also

References

  1. ↑ Li S, Anzai Y, Kinoshita K, Kato F, Sherman DH. Functional analysis of MycE and MycF, two O-methyltransferases involved in the biosynthesis of mycinamicin macrolide antibiotics. Chembiochem. 2009 May 25;10(8):1297-301. doi: 10.1002/cbic.200900088. PMID:19415708 doi:http://dx.doi.org/10.1002/cbic.200900088
  2. ↑ Akey DL, Li S, Konwerski JR, Confer LA, Bernard SM, Anzai Y, Kato F, Sherman DH, Smith JL. A new structural form in the SAM/metal-dependent omethyltransferase family: MycE from the mycinamicin biosynthetic pathway. J Mol Biol. 2011 Oct 21;413(2):438-50. Epub 2011 Aug 23. PMID:21884704 doi:10.1016/j.jmb.2011.08.040

3ssm, resolution 2.25Å

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