6pqf: Difference between revisions

(5 intermediate revisions by the same user not shown)

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6pqf is ~~ON HOLD~~

==Solution structure of OlvA(BCS)==

== Structural highlights ==

<table><tr><td colspan='2'>[[6pqf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_olivaceus Streptomyces olivaceus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PQF FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene>, <scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</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=6pqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pqf OCA], [https://pdbe.org/6pqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pqf RCSB], [https://www.ebi.ac.uk/pdbsum/6pqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pqf ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Lanthipeptides represent a large class of cyclic natural products defined by the presence of lanthionine (Lan) and methyllanthionine (MeLan) cross-links. With the advances in DNA sequencing technologies and genome mining tools, new biosynthetic enzymes capable of installing unusual structural features are continuously being discovered. In this study, we investigated an O-methyltransferase that is a member of the most prominent auxiliary enzyme family associated with class I lanthipeptide biosynthetic gene clusters. Despite the prevalence of these enzymes, their function has not been established. Herein, we demonstrate that the O-methyltransferase OlvSA encoded in the olv gene cluster from Streptomyces olivaceus NRRL B-3009 catalyzes the rearrangement of a highly conserved aspartate residue to a beta-amino acid, isoaspartate, in the lanthipeptide OlvA(BCSA). We elucidated the NMR solution structure of the GluC-digested peptide, OlvA(BCSA)(GluC), which revealed a unique ring topology comprising four interlocking rings and positions the isoaspartate residue in a solvent exposed loop that is stabilized by a MeLan ring. Gas chromatography-mass spectrometry analysis further indicated that OlvA(BCSA) contains two dl-MeLan rings and two Lan rings with an unusual ll-stereochemistry. Lastly, in vitro reconstitution of OlvSA activity showed that it is a leader peptide-independent and S-adenosyl methionine-dependent O-methyltransferase that mediates the conversion of a highly conserved aspartate residue in a cyclic substrate into a succinimide, which is hydrolyzed to generate an Asp or isoAsp containing peptide. This overall transformation converts an alpha-amino acid into a beta-amino acid in a ribosomally synthesized peptide, via an electrophilic intermediate that may be the intended product.

~~Authors:~~ Acedo, ~~J.Z.~~, van der Donk~~, W~~.A.

O-Methyltransferase-Mediated Incorporation of a beta-Amino Acid in Lanthipeptides.,Acedo JZ, Bothwell IR, An L, Trouth A, Frazier C, van der Donk WA J Am Chem Soc. 2019 Oct 15. doi: 10.1021/jacs.9b07396. PMID:31568727<ref>PMID:31568727</ref>

~~Description~~: ~~Solution structure of OlvA(BCS)~~

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

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Acedo~~, J.Z~~]]

[[Category: Van ~~Der~~ Donk~~, W.A~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Streptomyces olivaceus]]

[[Category: Acedo JZ]]

[[Category: Van der Donk WA]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6pqf is ON HOLD
+==Solution structure of OlvA(BCS)==
+<StructureSection load='6pqf' size='340' side='right'caption='[[6pqf]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6pqf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_olivaceus Streptomyces olivaceus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PQF FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene>, <scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</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=6pqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pqf OCA], [https://pdbe.org/6pqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pqf RCSB], [https://www.ebi.ac.uk/pdbsum/6pqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pqf ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Lanthipeptides represent a large class of cyclic natural products defined by the presence of lanthionine (Lan) and methyllanthionine (MeLan) cross-links. With the advances in DNA sequencing technologies and genome mining tools, new biosynthetic enzymes capable of installing unusual structural features are continuously being discovered. In this study, we investigated an O-methyltransferase that is a member of the most prominent auxiliary enzyme family associated with class I lanthipeptide biosynthetic gene clusters. Despite the prevalence of these enzymes, their function has not been established. Herein, we demonstrate that the O-methyltransferase OlvSA encoded in the olv gene cluster from Streptomyces olivaceus NRRL B-3009 catalyzes the rearrangement of a highly conserved aspartate residue to a beta-amino acid, isoaspartate, in the lanthipeptide OlvA(BCSA). We elucidated the NMR solution structure of the GluC-digested peptide, OlvA(BCSA)(GluC), which revealed a unique ring topology comprising four interlocking rings and positions the isoaspartate residue in a solvent exposed loop that is stabilized by a MeLan ring. Gas chromatography-mass spectrometry analysis further indicated that OlvA(BCSA) contains two dl-MeLan rings and two Lan rings with an unusual ll-stereochemistry. Lastly, in vitro reconstitution of OlvSA activity showed that it is a leader peptide-independent and S-adenosyl methionine-dependent O-methyltransferase that mediates the conversion of a highly conserved aspartate residue in a cyclic substrate into a succinimide, which is hydrolyzed to generate an Asp or isoAsp containing peptide. This overall transformation converts an alpha-amino acid into a beta-amino acid in a ribosomally synthesized peptide, via an electrophilic intermediate that may be the intended product.
-Authors: Acedo, J.Z., van der Donk, W.A.
+O-Methyltransferase-Mediated Incorporation of a beta-Amino Acid in Lanthipeptides.,Acedo JZ, Bothwell IR, An L, Trouth A, Frazier C, van der Donk WA J Am Chem Soc. 2019 Oct 15. doi: 10.1021/jacs.9b07396. PMID:31568727<ref>PMID:31568727</ref>
-Description: Solution structure of OlvA(BCS)
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Acedo, J.Z]]
+<div class="pdbe-citations 6pqf" style="background-color:#fffaf0;"></div>
-[[Category: Van Der Donk, W.A]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptomyces olivaceus]]
+[[Category: Acedo JZ]]
+[[Category: Van der Donk WA]]