6trp: Difference between revisions

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<StructureSection load='6trp' size='340' side='right'caption='[[6trp]]' scene=''>
<StructureSection load='6trp' size='340' side='right'caption='[[6trp]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6trp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenorhabdus_bovienii_SS-2004 Xenorhabdus bovienii SS-2004]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TRP FirstGlance]. <br>
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TRP FirstGlance]. <br>
</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=6trp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trp OCA], [https://pdbe.org/6trp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6trp RCSB], [https://www.ebi.ac.uk/pdbsum/6trp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6trp ProSAT]</span></td></tr>
</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=6trp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6trp OCA], [https://pdbe.org/6trp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6trp RCSB], [https://www.ebi.ac.uk/pdbsum/6trp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6trp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D3V3G3_XENBS D3V3G3_XENBS] [https://www.uniprot.org/uniprot/D3V3G2_XENBS D3V3G2_XENBS]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Xenorhabdus bovienii SS-2004]]
[[Category: Bode HB]]
[[Category: Bode HB]]
[[Category: Duchardt-Ferner E]]
[[Category: Duchardt-Ferner E]]

Latest revision as of 09:09, 19 June 2024

Solution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDDSolution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDD

Structural highlights

Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Nonribosomal peptide synthetases (NRPSs) produce a wide variety of different natural products from amino acid precursors. In contrast to single protein NRPS, the NRPS of the bacterium Xenorhabdus bovienii producing the peptide-antimicrobial-Xenorhabdus (PAX) peptide consists of three individual proteins (PaxA/B/C), which interact with each other noncovalently in a linear fashion. The specific interactions between the three different proteins in this NRPS system are mediated by short C- and N-terminal docking domains ((C/N)DDs). Here, we investigate the structural basis for the specific interaction between the (C)DD from the protein PaxB and the (N)DD from PaxC. The isolated DD peptides feature transient alpha-helical conformations in the absence of the respective DD partner. Isothermal titration calorimetry (ITC) and nuclear magnetic resonance (NMR) titration experiments showed that the two isolated DDs bind to each other and form a structurally well-defined complex with a dissociation constant in the micromolar range as is typical for many DD interactions. Artificial linking of this DD pair via a flexible glycine-serine (GS) linker enabled us to solve the structure of the DD complex by NMR spectroscopy. In the complex, the two DDs interact with each other by forming a three helix bundle arranged in an overall coiled-coil motif. Key interacting residues were identified in mutagenesis experiments. Overall, our structure of the PaxB (C)DD/PaxC (N)DD complex represents an architecturally new type of DD interaction motif.

A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase from Xenorhabdus bovienii.,Watzel J, Hacker C, Duchardt-Ferner E, Bode HB, Wohnert J ACS Chem Biol. 2020 Apr 17;15(4):982-989. doi: 10.1021/acschembio.9b01022. Epub, 2020 Mar 25. PMID:32167274[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Watzel J, Hacker C, Duchardt-Ferner E, Bode HB, Wohnert J. A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase from Xenorhabdus bovienii. ACS Chem Biol. 2020 Apr 17;15(4):982-989. doi: 10.1021/acschembio.9b01022. Epub, 2020 Mar 25. PMID:32167274 doi:http://dx.doi.org/10.1021/acschembio.9b01022
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