6ewt: Difference between revisions
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<StructureSection load='6ewt' size='340' side='right'caption='[[6ewt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='6ewt' size='340' side='right'caption='[[6ewt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ewt]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6ewt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cip_109067 Cip 109067]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EWT FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=6ewt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ewt OCA], [https://pdbe.org/6ewt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ewt RCSB], [https://www.ebi.ac.uk/pdbsum/6ewt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ewt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 10:40, 25 June 2021
Solution Structure of Rhabdopeptide NRPS Docking Domain Kj12B-NDDSolution Structure of Rhabdopeptide NRPS Docking Domain Kj12B-NDD
Structural highlights
Publication Abstract from PubMedSeveral peptides in clinical use are derived from non-ribosomal peptide synthetases (NRPS). In these systems multiple NRPS subunits interact with each other in a specific linear order mediated by specific docking domains (DDs), whose structures are not known yet, to synthesize well-defined peptide products. In contrast to classical NRPSs, single-module NRPS subunits responsible for the generation of rhabdopeptide/xenortide-like peptides (RXPs) can act in different order depending on subunit stoichiometry thereby producing peptide libraries. To define the basis for their unusual interaction patterns, we determine the structures of all N-terminal DDs ((N)DDs) as well as of an (N)DD-(C)DD complex and characterize all putative DD interactions thermodynamically for such a system. Key amino acid residues for DD interactions are identified that upon their exchange change the DD affinity and result in predictable changes in peptide production. Recognition rules for DD interactions are identified that also operate in other megasynthase complexes. Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS.,Hacker C, Cai X, Kegler C, Zhao L, Weickhmann AK, Wurm JP, Bode HB, Wohnert J Nat Commun. 2018 Oct 19;9(1):4366. doi: 10.1038/s41467-018-06712-1. PMID:30341296[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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