4oqe
From Proteopedia
(Difference between revisions)
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- | + | ==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=''> | |
- | + | == 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> | |
- | ==Function== | + | </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> |
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oqd|4oqd]]</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://www.rcsb.org/pdb/explore.do?structureId=4oqe RCSB], [http://www.ebi.ac.uk/pdbsum/4oqe PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == 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> | [[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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:24512254</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: DTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase]] | [[Category: DTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase]] | ||
- | [[Category: Holden, H M | + | [[Category: Holden, H M]] |
- | [[Category: Thoden, J B | + | [[Category: Thoden, J B]] |
[[Category: N-methyltransferase]] | [[Category: N-methyltransferase]] | ||
[[Category: S-adenosylmethionine]] | [[Category: S-adenosylmethionine]] | ||
[[Category: Sam methyltransferase]] | [[Category: Sam methyltransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 23:59, 24 December 2014
Crystal structure of the tylM1 N,N-dimethyltransferase in complex with SAH and TDP-Fuc3NMe
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