2mw3: Difference between revisions

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'''Unreleased structure'''


The entry 2mw3 is ON HOLD  until Paper Publication
==Solution NMR structure of the lasso peptide streptomonomicin==
<StructureSection load='2mw3' size='340' side='right'caption='[[2mw3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mw3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomonospora_alba Streptomonospora alba]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MW3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=2mw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw3 OCA], [https://pdbe.org/2mw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mw3 RCSB], [https://www.ebi.ac.uk/pdbsum/2mw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mw3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0C2JEQ8_9ACTN A0A0C2JEQ8_9ACTN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Natural products are the most historically significant source of compounds for drug development. However, unacceptably high rates of compound rediscovery associated with large-scale screening of common microbial producers have resulted in the abandonment of many natural product drug discovery efforts, despite the increasing prevalence of clinically problematic antibiotic resistance. Screening of underexplored taxa represents one strategy to avoid rediscovery. Herein we report the discovery, isolation, and structural elucidation of streptomonomicin (STM), an antibiotic lasso peptide from Streptomonospora alba, and report the genome for its producing organism. STM-resistant clones of Bacillus anthracis harbor mutations to walR, the gene encoding a response regulator for the only known widely distributed and essential two-component signal transduction system in Firmicutes. To the best of our knowledge, Streptomonospora had been hitherto biosynthetically and genetically uncharacterized, with STM being the first reported compound from the genus. Our results demonstrate that understudied microbes remain fruitful reservoirs for the rapid discovery of novel, bioactive natural products.


Authors: Tietz, J.I., Zhu, L., Mitchell, D.A., Metelev, M., Melby, J.O., Blair, P.M., Livnat, I., Severinov, K.
Structure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic Actinomycete.,Metelev M, Tietz JI, Melby JO, Blair PM, Zhu L, Livnat I, Severinov K, Mitchell DA Chem Biol. 2015 Jan 14. pii: S1074-5521(14)00452-9. doi:, 10.1016/j.chembiol.2014.11.017. PMID:25601074<ref>PMID:25601074</ref>


Description: Solution NMR structure of the lasso peptide streptomonomicin
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mw3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomonospora alba]]
[[Category: Blair PM]]
[[Category: Livnat I]]
[[Category: Melby JO]]
[[Category: Metelev M]]
[[Category: Mitchell DA]]
[[Category: Severinov K]]
[[Category: Tietz JI]]
[[Category: Zhu L]]

Latest revision as of 08:22, 17 October 2024

Solution NMR structure of the lasso peptide streptomonomicinSolution NMR structure of the lasso peptide streptomonomicin

Structural highlights

2mw3 is a 1 chain structure with sequence from Streptomonospora alba. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 15 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0C2JEQ8_9ACTN

Publication Abstract from PubMed

Natural products are the most historically significant source of compounds for drug development. However, unacceptably high rates of compound rediscovery associated with large-scale screening of common microbial producers have resulted in the abandonment of many natural product drug discovery efforts, despite the increasing prevalence of clinically problematic antibiotic resistance. Screening of underexplored taxa represents one strategy to avoid rediscovery. Herein we report the discovery, isolation, and structural elucidation of streptomonomicin (STM), an antibiotic lasso peptide from Streptomonospora alba, and report the genome for its producing organism. STM-resistant clones of Bacillus anthracis harbor mutations to walR, the gene encoding a response regulator for the only known widely distributed and essential two-component signal transduction system in Firmicutes. To the best of our knowledge, Streptomonospora had been hitherto biosynthetically and genetically uncharacterized, with STM being the first reported compound from the genus. Our results demonstrate that understudied microbes remain fruitful reservoirs for the rapid discovery of novel, bioactive natural products.

Structure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic Actinomycete.,Metelev M, Tietz JI, Melby JO, Blair PM, Zhu L, Livnat I, Severinov K, Mitchell DA Chem Biol. 2015 Jan 14. pii: S1074-5521(14)00452-9. doi:, 10.1016/j.chembiol.2014.11.017. PMID:25601074[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Metelev M, Tietz JI, Melby JO, Blair PM, Zhu L, Livnat I, Severinov K, Mitchell DA. Structure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic Actinomycete. Chem Biol. 2015 Jan 14. pii: S1074-5521(14)00452-9. doi:, 10.1016/j.chembiol.2014.11.017. PMID:25601074 doi:http://dx.doi.org/10.1016/j.chembiol.2014.11.017
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