5v7o: Difference between revisions

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'''Unreleased structure'''


The entry 5v7o is ON HOLD
==Crystal Structure of NosK from Streptomyces actuosus==
<StructureSection load='5v7o' size='340' side='right' caption='[[5v7o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5v7o]] is a 1 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V7O FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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://oca.weizmann.ac.il/oca-docs/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>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Booker, S.J., Boal, A.K, Grove, T.L., Badding, E.D.
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>


Description: Crystal Structure of NosK from Streptomyces actuosus
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Booker, S.J]]
<div class="pdbe-citations 5v7o" style="background-color:#fffaf0;"></div>
[[Category: Boal, A.K, Grove, T.L]]
== References ==
[[Category: Badding, E.D]]
<references/>
__TOC__
</StructureSection>
[[Category: Badding, E D]]
[[Category: Boal, A K]]
[[Category: Booker, S J]]
[[Category: Grove, T L]]
[[Category: Acyltransferase]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Nosiheptide]]
[[Category: Transferase]]
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