View source for 7b2b


==Solution structure of a non-covalent extended docking domain complex of the Pax NRPS: PaxA T1-CDD/PaxB NDD==
<StructureSection load='7b2b' size='340' side='right'caption='[[7b2b]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7b2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenorhabdus_cabanillasii Xenorhabdus cabanillasii] and [https://en.wikipedia.org/wiki/Xenorhabdus_cabanillasii_JM26 Xenorhabdus cabanillasii JM26]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B2B 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=7b2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b2b OCA], [https://pdbe.org/7b2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b2b RCSB], [https://www.ebi.ac.uk/pdbsum/7b2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b2b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W1J0W9_9GAMM W1J0W9_9GAMM] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7b2b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenorhabdus cabanillasii]]
[[Category: Xenorhabdus cabanillasii JM26]]
[[Category: Bode HB]]
[[Category: Duchardt-Ferner E]]
[[Category: Sarawi S]]
[[Category: Watzel J]]
[[Category: Woehnert J]]