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6uak

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Current revision (14:56, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6uak' size='340' side='right'caption='[[6uak]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='6uak' size='340' side='right'caption='[[6uak]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6uak]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_c6a11 Lachnospiraceae bacterium c6a11]. 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>
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<table><tr><td colspan='2'>[[6uak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_C6A11 Lachnospiraceae bacterium C6A11]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6UAK FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEO87_04690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1410622 Lachnospiraceae bacterium C6A11])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6uak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uak OCA], [https://pdbe.org/6uak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uak RCSB], [https://www.ebi.ac.uk/pdbsum/6uak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uak ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A3D0LE54_9FIRM A0A3D0LE54_9FIRM]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6uak" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lachnospiraceae bacterium c6a11]]
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[[Category: Lachnospiraceae bacterium C6A11]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Estrada, P]]
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[[Category: Estrada P]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Methyltransferase]]
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[[Category: Ripp]]
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[[Category: Transferase]]
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Current revision

LahSb - C-terminal methyltransferase involved in RiPP biosynthesis

PDB ID 6uak

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