6uak: Difference between revisions
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The | ==LahSb - C-terminal methyltransferase involved in RiPP biosynthesis== | ||
<StructureSection load='6uak' size='340' side='right'caption='[[6uak]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6uak]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UAK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=6uak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uak OCA], [http://pdbe.org/6uak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uak RCSB], [http://www.ebi.ac.uk/pdbsum/6uak PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uak ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
As a result of the exponential increase in genomic data, discovery of novel ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) has progressed rapidly in the past decade. The lanthipeptides are a major subset of RiPPs. Through genome mining we identified a novel lanthipeptide biosynthetic gene cluster (lah) from Lachnospiraceae bacterium C6A11, an anaerobic bacterium that is a member of the human microbiota and which is implicated in the development of host disease states such as type 2 diabetes and resistance to Clostridium difficile colonization. The lah cluster encodes at least seven putative precursor peptides and multiple post-translational modification (PTM) enzymes. Two unusual class II lanthipeptide synthetases LahM1/M2 and a substrate-tolerant S-adenosyl-l-methionine (SAM)-dependent methyltransferase LahSB are biochemically characterized in this study. We also present the crystal structure of LahSB in complex with product S-adenosylhomocysteine. This study sets the stage for further exploration of the final products of the lah pathway as well as their potential physiological functions in human/animal gut microbiota. | |||
Characterization of a Dehydratase and Methyltransferase in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides in Lachnospiraceae.,Huo L, Zhao X, Acedo JZ, Estrada P, Nair SK, van der Donk WA Chembiochem. 2019 Sep 18. doi: 10.1002/cbic.201900483. PMID:31532570<ref>PMID:31532570</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6uak" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Estrada, P]] | [[Category: Estrada, P]] | ||
[[Category: Nair, S | [[Category: Nair, S K]] | ||
[[Category: Methyltransferase]] | |||
[[Category: Ripp]] | |||
[[Category: Transferase]] | |||
Revision as of 08:22, 4 December 2019
LahSb - C-terminal methyltransferase involved in RiPP biosynthesis
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