7b2f: Difference between revisions
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The | ==Solution structure of the Pax NRPS docking domain PaxB NDD== | ||
<StructureSection load='7b2f' size='340' side='right'caption='[[7b2f]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B2F FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=7b2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b2f OCA], [https://pdbe.org/7b2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b2f RCSB], [https://www.ebi.ac.uk/pdbsum/7b2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b2f ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Non-ribosomal peptide synthetases (NRPS) produce natural products from amino acid building blocks. They often consist of multiple polypeptide chains which assemble in a specific linear order via specialized N- and C-terminal docking domains ((N/C) DDs). Typically, docking domains function independently from other domains in NRPS assembly. Thus, docking domain replacements enable the assembly of "designer" NRPS from proteins that normally do not interact. The multiprotein "peptide-antimicrobial-Xenorhabdus" (PAX) peptide-producing PaxS NRPS is assembled from the three proteins PaxA, PaxB and PaxC. Herein, we show that the small (C) DD of PaxA cooperates with its preceding thiolation (T1 ) domain to bind the (N) DD of PaxB with very high affinity, establishing a structural and thermodynamical basis for this unprecedented docking interaction, and we test its functional importance in vivo in a truncated PaxS assembly line. Similar docking interactions are apparently present in other NRPS systems. | |||
Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS.,Watzel J, Duchardt-Ferner E, Sarawi S, Bode HB, Wohnert J Angew Chem Int Ed Engl. 2021 Jun 14;60(25):14171-14178. doi:, 10.1002/anie.202103498. Epub 2021 May 14. PMID:33876501<ref>PMID:33876501</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7b2f" style="background-color:#fffaf0;"></div> | ||
[[Category: Duchardt-Ferner | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Bode HB]] | |||
[[Category: Duchardt-Ferner E]] | |||
[[Category: Sarawi S]] | |||
[[Category: Watzel J]] | |||
[[Category: Woehnert J]] | |||