5ttb: Difference between revisions
New page: '''Unreleased structure''' The entry 5ttb is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==Solution structure of apo ArCP from yersiniabactin synthetase== | |||
<StructureSection load='5ttb' size='340' side='right'caption='[[5ttb]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ttb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TTB 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=5ttb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttb OCA], [https://pdbe.org/5ttb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ttb RCSB], [https://www.ebi.ac.uk/pdbsum/5ttb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ttb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0S2UWU4_YERPE A0A0S2UWU4_YERPE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nonribosomal peptide (NRP) synthesis involves the interplay between covalent protein modifications, conformational fluctuations, catalysis, and transient protein-protein interactions. Delineating the mechanisms involved in orchestrating these various processes will deepen our understanding of domain-domain communication in nonribosomal peptide synthetases (NRPSs) and lay the groundwork for the rational reengineering of NRPSs by swapping domains handling different substrates to generate novel natural products. While many structural and biochemical studies of NRPSs exist, few studies have focused on the energetics and dynamics governing the interactions in these systems. Here, we present detailed binding studies of an adenylation domain and its partner carrier protein in apo, holo, and substrate-loaded forms. Results from fluorescence anisotropy, isothermal titration calorimetry, and NMR titrations indicated that covalent modifications to a carrier protein modulate domain communication, suggesting that chemical modifications to carrier proteins during NRPS synthesis may impart directionality to sequential NRPS domain interactions. Comparison of the structure and dynamics of an apo aryl carrier protein with those of its modified forms revealed structural fluctuations induced by post-translational modifications and mediated by modulations of protein dynamics. The results provide a comprehensive molecular description of a carrier protein throughout its life cycle and demonstrate how a network of dynamic residues can propagate the molecular impact of chemical modifications throughout a protein and influence its affinity towards partner domains. | |||
Molecular Impact of Covalent Modifications on Nonribosomal Peptide Synthetase Carrier Protein Communication.,Goodrich AC, Meyers DJ, Frueh DP J Biol Chem. 2017 Apr 28. pii: jbc.M116.766220. doi: 10.1074/jbc.M116.766220. PMID:28455448<ref>PMID:28455448</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ttb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Yersinia pestis]] | |||
[[Category: Frueh DP]] | |||
[[Category: Goodrich AC]] | |||
Latest revision as of 13:25, 14 June 2023
Solution structure of apo ArCP from yersiniabactin synthetaseSolution structure of apo ArCP from yersiniabactin synthetase
Structural highlights
FunctionPublication Abstract from PubMedNonribosomal peptide (NRP) synthesis involves the interplay between covalent protein modifications, conformational fluctuations, catalysis, and transient protein-protein interactions. Delineating the mechanisms involved in orchestrating these various processes will deepen our understanding of domain-domain communication in nonribosomal peptide synthetases (NRPSs) and lay the groundwork for the rational reengineering of NRPSs by swapping domains handling different substrates to generate novel natural products. While many structural and biochemical studies of NRPSs exist, few studies have focused on the energetics and dynamics governing the interactions in these systems. Here, we present detailed binding studies of an adenylation domain and its partner carrier protein in apo, holo, and substrate-loaded forms. Results from fluorescence anisotropy, isothermal titration calorimetry, and NMR titrations indicated that covalent modifications to a carrier protein modulate domain communication, suggesting that chemical modifications to carrier proteins during NRPS synthesis may impart directionality to sequential NRPS domain interactions. Comparison of the structure and dynamics of an apo aryl carrier protein with those of its modified forms revealed structural fluctuations induced by post-translational modifications and mediated by modulations of protein dynamics. The results provide a comprehensive molecular description of a carrier protein throughout its life cycle and demonstrate how a network of dynamic residues can propagate the molecular impact of chemical modifications throughout a protein and influence its affinity towards partner domains. Molecular Impact of Covalent Modifications on Nonribosomal Peptide Synthetase Carrier Protein Communication.,Goodrich AC, Meyers DJ, Frueh DP J Biol Chem. 2017 Apr 28. pii: jbc.M116.766220. doi: 10.1074/jbc.M116.766220. PMID:28455448[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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