View source for 9dk2


==Lexapeptide dehydratase complex LxmKY, ATP bound==
<StructureSection load='9dk2' size='340' side='right'caption='[[9dk2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9dk2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rochei Streptomyces rochei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DK2 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=9dk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dk2 OCA], [https://pdbe.org/9dk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dk2 RCSB], [https://www.ebi.ac.uk/pdbsum/9dk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dk2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0K1TP15_STRRO A0A0K1TP15_STRRO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lanthipeptides are ribosomally synthesized and post-translationally modified peptides that bear the characteristic lanthionine (Lan) or methyllanthionine (MeLan) thioether linkages. (Me)Lan moieties bestow lanthipeptides with robust stability and diverse antimicrobial, anticancer, and antiallodynic activities. Installation of (Me)Lan requires dehydration of serine and threonine residues to 2,3-dehydroalanine (Dha) and (Z)-2,3-dehydrobutyrine (Dhb), respectively. LxmK and LxmY enzymes comprise the biosynthetic machinery of a newly discovered class V lanthipeptide, lexapeptide, and are proposed to catalyze the dehydration of serine and threonine residues in the precursor peptide. We demonstrate that LxmK and LxmY form a stable dehydratase complex to dehydrate precursor peptides. In addition, we present crystal structures of the LxmKY heterodimer, revealing structural and mechanistic features that enable iterative phosphorylation and elimination by the LxmKY complex. These findings provide molecular insights into class V lanthionine synthetases and lay the foundation for their applications as enzymatic tools in the biosynthesis of exquisitely modified peptides.

A Stable Dehydratase Complex Catalyzes the Formation of Dehydrated Amino Acids in a Class V Lanthipeptide.,Randall GT, Grant-Mackie ES, Chunkath S, Williams ET, Middleditch MJ, Tao M, Harris PWR, Brimble MA, Bashiri G ACS Chem Biol. 2024 Nov 25. doi: 10.1021/acschembio.4c00637. PMID:39586055<ref>PMID:39586055</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9dk2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces rochei]]
[[Category: Bashiri G]]
[[Category: Randall GT]]