View source for 7ltr


==Structure of the heteromeric complex between the alpha-N-methyltransferase (SonM) and a truncated construct of the RiPP precursor (SonA) (with SAM)==
<StructureSection load='7ltr' size='340' side='right'caption='[[7ltr]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ltr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LTR 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=7ltr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ltr OCA], [https://pdbe.org/7ltr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ltr RCSB], [https://www.ebi.ac.uk/pdbsum/7ltr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ltr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8EGW3_SHEON Q8EGW3_SHEON] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptide backbone alpha-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides. Borosin natural product pathways are the only known ribosomally encoded and posttranslationally modified peptides (RiPPs) pathways to incorporate backbone alpha-N-methylations on translated peptides. Here we report the discovery of type IV borosin natural product pathways (termed 'split borosins'), featuring an iteratively acting alpha-N-methyltransferase and separate precursor peptide substrate from the metal-respiring bacterium Shewanella oneidensis. A series of enzyme-precursor complexes reveal multiple conformational states for both alpha-N-methyltransferase and substrate. Along with mutational and kinetic analyses, our results give rare context into potential strategies for iterative maturation of RiPPs.

Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis.,Miller FS, Crone KK, Jensen MR, Shaw S, Harcombe WR, Elias MH, Freeman MF Nat Commun. 2021 Sep 9;12(1):5355. doi: 10.1038/s41467-021-25575-7. PMID:34504067<ref>PMID:34504067</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ltr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Shewanella oneidensis MR-1]]
[[Category: Crone KK]]
[[Category: Elias M]]
[[Category: Freeman MF]]
[[Category: Harcombe WR]]
[[Category: Jensen MR]]
[[Category: Miller FS]]
[[Category: Shaw S]]