6zsu: Difference between revisions

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'''Unreleased structure'''


The entry 6zsu is ON HOLD
==Structure of crocagin biosynthetic protein CgnE==
<StructureSection load='6zsu' size='340' side='right'caption='[[6zsu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6zsu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chondromyces_crocatus Chondromyces crocatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZSU FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=6zsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zsu OCA], [https://pdbe.org/6zsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zsu RCSB], [https://www.ebi.ac.uk/pdbsum/6zsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zsu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0K1ECI7_CHOCO A0A0K1ECI7_CHOCO]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribosomally synthesized and post-translationally modified peptide natural products have provided many highly unusual scaffolds. This includes the intriguing alkaloids crocagins, which possess a tetracyclic core structure and whose biosynthesis has remained enigmatic. Here we use in vitro experiments to demonstrate that three proteins, CgnB, CgnC and CgnE, are sufficient for the production of the hallmark tetracyclic crocagin core from the precursor peptide CgnA. The crystal structures of the homologues CgnB and CgnE reveal them to be the founding members of a peptide-binding protein family and allow us to rationalize their distinct functions. We further show that the hydrolase CgnD liberates the crocagin core scaffold, which is subsequently N-methylated by CgnL. These insights allow us to propose a biosynthetic scheme for crocagins. Bioinformatic analyses based on these data led to the discovery of related biosynthetic pathways that may provide access to a structurally diverse family of peptide-derived pyrroloindoline alkaloids.


Authors:  
Unusual peptide-binding proteins guide pyrroloindoline alkaloid formation in crocagin biosynthesis.,Adam S, Zheng D, Klein A, Volz C, Mullen W, Shirran SL, Smith BO, Kalinina OV, Muller R, Koehnke J Nat Chem. 2023 Apr;15(4):560-568. doi: 10.1038/s41557-023-01153-w. Epub 2023 Mar , 9. PMID:36894702<ref>PMID:36894702</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6zsu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chondromyces crocatus]]
[[Category: Large Structures]]
[[Category: Adam S]]
[[Category: Koehnke J]]

Latest revision as of 13:23, 6 November 2024

Structure of crocagin biosynthetic protein CgnE

6zsu, resolution 2.00Å

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