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5thy

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Current revision (15:41, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5thy' size='340' side='right'caption='[[5thy]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='5thy' size='340' side='right'caption='[[5thy]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5thy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_majuscula_3l Lyngbya majuscula 3l]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5THY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5THY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5thy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorena_producens_3L Moorena producens 3L]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5THY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5THY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.087&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5thz|5thz]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5thy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5thy OCA], [https://pdbe.org/5thy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5thy RCSB], [https://www.ebi.ac.uk/pdbsum/5thy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5thy ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYNGBM3L_74460 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=489825 Lyngbya majuscula 3L])</td></tr>
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<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=5thy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5thy OCA], [http://pdbe.org/5thy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5thy RCSB], [http://www.ebi.ac.uk/pdbsum/5thy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5thy ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F4Y426_9CYAN F4Y426_9CYAN]
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Polyketide metabolites produced by modular type I polyketide synthases (PKS) acquire their chemical diversity through the variety of catalytic domains within modules of the pathway. Methyltransferases are among the least characterized of the catalytic domains common to PKS systems. We determined the domain boundaries and characterized the activity of a PKS C-methyltransferase (C-MT) from the curacin A biosynthetic pathway. The C-MT catalyzes S-adenosylmethionine-dependent methyl transfer to the alpha-position of beta-ketoacyl substrates linked to acyl carrier protein (ACP) or a small-molecule analog, but does not act on beta-hydroxyacyl substrates or malonyl-ACP. Key catalytic residues conserved in both bacterial and fungal PKS C-MTs were identified in a 2-A crystal structure and validated biochemically. Analysis of the structure and the sequences bordering the C-MT provides insight into the positioning of this domain within complete PKS modules.
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Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase.,Skiba MA, Sikkema AP, Fiers WD, Gerwick WH, Sherman DH, Aldrich CC, Smith JL ACS Chem Biol. 2016 Oct 10. PMID:27723289<ref>PMID:27723289</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5thy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lyngbya majuscula 3l]]
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[[Category: Moorena producens 3L]]
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[[Category: Skiba, M A]]
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[[Category: Skiba MA]]
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[[Category: Smith, J L]]
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[[Category: Smith JL]]
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[[Category: Lyase]]
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[[Category: Methyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of SeMet-Substituted CurJ carbon methyltransferase

PDB ID 5thy

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