View source for 7wj6


==Crystal Structure of the Kinase Domain of a Class III Lanthipeptide Synthetase CurKC==
<StructureSection load='7wj6' size='340' side='right'caption='[[7wj6]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wj6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata_DSM_43183 Thermomonospora curvata DSM 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WJ6 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]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7wj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wj6 OCA], [https://pdbe.org/7wj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wj6 RCSB], [https://www.ebi.ac.uk/pdbsum/7wj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wj6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D1ABX1_THECD D1ABX1_THECD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Class III lanthipeptide synthetases catalyze the formation of lanthionine/methyllanthionine and labionin crosslinks. We present here the 2.40 A resolution structure of the kinase domain of a class III lanthipeptide synthetase CurKC from the biosynthesis of curvopeptin. A unique structural subunit for leader binding, named leader recognition domain (LRD), was identified. The LRD of CurKC is responsible for the recognition of the leader peptide and for mediating interactions between the lyase and kinase domains. LRDs are highly conserved among the kinase domains of class III and class IV lanthipeptide synthetases. The discovery of LRDs provides insight into the substrate recognition and domain organization in multidomain lanthipeptide synthetases.

Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.,Huang S, Wang Y, Cai C, Xiao X, Liu S, Ma Y, Xie X, Liang Y, Chen H, Zhu J, Hegemann JD, Yao H, Wei W, Wang H Angew Chem Int Ed Engl. 2022 Nov 7;61(45):e202211382. doi:, 10.1002/anie.202211382. Epub 2022 Oct 7. PMID:36102578<ref>PMID:36102578</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wj6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomonospora curvata DSM 43183]]
[[Category: Huang S]]
[[Category: Wang H]]