|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Fuc3NMe== | | ==Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Fuc3NMe== |
| - | <StructureSection load='4oqe' size='340' side='right' caption='[[4oqe]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4oqe' size='340' side='right'caption='[[4oqe]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oqe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_fradii"_(sic)_waksman_and_curtis_1916 "actinomyces fradii" (sic) waksman and curtis 1916]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OQE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oqe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_fradiae Streptomyces fradiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OQE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MMF:DTDP-3-N-METHYLAMINO-3,6-DIDEOXYGALACTOSE'>MMF</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MMF:DTDP-3-N-METHYLAMINO-3,6-DIDEOXYGALACTOSE'>MMF</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oqd|4oqd]]</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=4oqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqe OCA], [https://pdbe.org/4oqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oqe RCSB], [https://www.ebi.ac.uk/pdbsum/4oqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqe ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tylM1, tylMI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1906 "Actinomyces fradii" (sic) Waksman and Curtis 1916])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose_N,N-dimethyltransferase dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.235 2.1.1.235] </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=4oqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqe OCA], [http://pdbe.org/4oqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oqe RCSB], [http://www.ebi.ac.uk/pdbsum/4oqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TYLM1_STRFR TYLM1_STRFR]] S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin. Involved in the last step in mycaminose biosynthesis by mediating dimethylation of the hexose C-3' amino group.<ref>PMID:9031628</ref> <ref>PMID:12119032</ref> <ref>PMID:21142177</ref> | + | [https://www.uniprot.org/uniprot/TYLM1_STRFR TYLM1_STRFR] S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin. Involved in the last step in mycaminose biosynthesis by mediating dimethylation of the hexose C-3' amino group.<ref>PMID:9031628</ref> <ref>PMID:12119032</ref> <ref>PMID:21142177</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: DTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Holden, H M]] | + | [[Category: Streptomyces fradiae]] |
| - | [[Category: Thoden, J B]] | + | [[Category: Holden HM]] |
| - | [[Category: N-methyltransferase]] | + | [[Category: Thoden JB]] |
| - | [[Category: S-adenosylmethionine]]
| + | |
| - | [[Category: Sam methyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TYLM1_STRFR S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin. Involved in the last step in mycaminose biosynthesis by mediating dimethylation of the hexose C-3' amino group.[1] [2] [3]
Publication Abstract from PubMed
The importance of unusual deoxysugars in biology has become increasingly apparent over the past decade. Some, for example, play key roles in the physiological activities of the natural products to which they are attached. Here we describe a study of TylM1, a dimethyltransferase from Streptomyces fradiae involved in the production of dTDP-mycaminose. From this investigation, the manner in which the enzyme binds its dimethylated product has been revealed. More significantly, by providing the enzyme with an alternative substrate, it was possible to produce a monomethylated product not observed in nature. This has important ramifications for the production of unique carbohydrates that may prove useful in drug design.
Production of a novel N-monomethylated dideoxysugar.,Thoden JB, Holden HM Biochemistry. 2014 Feb 25;53(7):1105-7. doi: 10.1021/bi500098a. Epub 2014 Feb 11. PMID:24512254[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gandecha AR, Large SL, Cundliffe E. Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome. Gene. 1997 Jan 15;184(2):197-203. PMID:9031628
- ↑ Chen H, Yamase H, Murakami K, Chang CW, Zhao L, Zhao Z, Liu HW. Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine. Biochemistry. 2002 Jul 23;41(29):9165-83. PMID:12119032
- ↑ Carney AE, Holden HM. Molecular Architecture of TylM1 from Streptomyces fradiae: an N,N-Dimethyltransferase Involved in the Production of dTDP-D-Mycaminose. Biochemistry. 2010 Dec 13. PMID:21142177 doi:10.1021/bi101733y
- ↑ Thoden JB, Holden HM. Production of a novel N-monomethylated dideoxysugar. Biochemistry. 2014 Feb 25;53(7):1105-7. doi: 10.1021/bi500098a. Epub 2014 Feb 11. PMID:24512254 doi:http://dx.doi.org/10.1021/bi500098a
|
