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| | <StructureSection load='5v7o' size='340' side='right'caption='[[5v7o]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5v7o' size='340' side='right'caption='[[5v7o]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v7o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_actuosus"_pinnert_et_al. "streptomyces actuosus" pinnert et al.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V7O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5V7O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v7o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_actuosus Streptomyces actuosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V7O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nosK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1885 "Streptomyces actuosus" Pinnert et al.])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5v7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v7o OCA], [http://pdbe.org/5v7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v7o RCSB], [http://www.ebi.ac.uk/pdbsum/5v7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v7o ProSAT]</span></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=5v7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v7o OCA], [https://pdbe.org/5v7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v7o RCSB], [https://www.ebi.ac.uk/pdbsum/5v7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v7o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/C6FX50_STRAS C6FX50_STRAS] |
| - | Nosiheptide (NOS) is a highly modified thiopeptide antibiotic that displays formidable in vitro activity against a variety of Gram-positive bacteria. In addition to a central hydroxypyridine ring, NOS contains several other modifications, including multiple thiazole rings, dehydro-amino acids, and a 2,4-dimethylindolic acid (DMIA) moiety, among others. The DMIA moiety is required for NOS efficacy and is synthesized from L-tryptophan in a series of reactions that have not been fully elucidated. Herein, we describe the role of NosJ-the product of an unannotated gene in the biosynthetic operon for NOS-as an acyl carrier protein that delivers 2-methylindolic acid (MIA) to NosK. We also reassign the role of NosI as the enzyme responsible for catalyzing the ATP-dependent activation of MIA and its attachment to the phosphopantetheine moiety of NosJ. Lastly, NosK catalyz-es the transfer of the MIA group from NosJ-MIA to a conserved serine residue (Ser102) on NosK. The x-ray crystal structure of NosK, solved to 2.3 A resolution, reveals that the protein is an alpha/beta-fold hydrolase. Ser102 interacts with Glu210 and His234 to form a catalytic triad located at the bottom of an open cleft that is large enough to accommodate the thiopeptide framework.
| + | |
| - | | + | |
| - | Rerouting the Pathway for the Biosynthesis of the Side Ring System of Nosiheptide: The Roles of NosI, NosJ, and NosK.,Badding E, Grove TL, Gadsby L, LaMattina J, Boal AK, Booker SJ J Am Chem Soc. 2017 Mar 27. doi: 10.1021/jacs.7b01497. PMID:28343381<ref>PMID:28343381</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5v7o" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces actuosus pinnert et al]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Badding, E D]] | + | [[Category: Streptomyces actuosus]] |
| - | [[Category: Boal, A K]] | + | [[Category: Badding ED]] |
| - | [[Category: Booker, S J]] | + | [[Category: Boal AK]] |
| - | [[Category: Grove, T L]] | + | [[Category: Booker SJ]] |
| - | [[Category: Acyltransferase]] | + | [[Category: Grove TL]] |
| - | [[Category: Alpha/beta hydrolase fold]]
| + | |
| - | [[Category: Nosiheptide]]
| + | |
| - | [[Category: Transferase]]
| + | |
