3sso: Difference between revisions

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 <StructureSection load='3sso' size='340' side='right'caption='[[3sso]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sso]] is a 6 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=3SSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sso]] is a 6 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=3SSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSO FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.895&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ssm|3ssm]], [[3ssn|3ssn]]</div></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 ([https://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=3sso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sso OCA], [https://pdbe.org/3sso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sso RCSB], [https://www.ebi.ac.uk/pdbsum/3sso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sso ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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>
-</div>
-<div class="pdbe-citations 3sso" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 27: / Line 17: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Micromonospora griseorubida]]
-[[Category: Large Structures]]
+[[Category: Akey DL]]
-[[Category: Akey, D L]]
+[[Category: Smith JL]]
-[[Category: Smith, J L]]
-[[Category: Macrolide]]
-[[Category: Methyltransferase]]
-[[Category: Natural product]]
-[[Category: Rossmann fold]]
-[[Category: Transferase]]