8fx7: Difference between revisions
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==Non-ribosomal PCP-C didomain (ester stabilised leucine) acceptor bound state== | |||
<StructureSection load='8fx7' size='340' side='right'caption='[[8fx7]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8fx7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FX7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YCT:2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl+(2~{S})-2-azanyl-4-methyl-pentanoate'>YCT</scene></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=8fx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fx7 OCA], [https://pdbe.org/8fx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fx7 RCSB], [https://www.ebi.ac.uk/pdbsum/8fx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fx7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q47NR9_THEFY Q47NR9_THEFY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nonribosomal peptide synthetases produce many important peptide natural products and are centred around carrier proteins (CPs) that deliver intermediates to various catalytic domains. We show that the replacement of CP substrate thioesters by stabilised ester analogues leads to active condensation domain complexes, whereas amide stabilisation generates non-functional complexes. | |||
Not always an innocent bystander: the impact of stabilised phosphopantetheine moieties when studying nonribosomal peptide biosynthesis.,Ho YTC, Kaczmarski JA, Tailhades J, Izore T, Steer DL, Schittenhelm RB, Tosin M, Jackson CJ, Cryle MJ Chem Commun (Camb). 2023 Jun 29;59(53):8234-8237. doi: 10.1039/d3cc01578e. PMID:37310188<ref>PMID:37310188</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8fx7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermobifida fusca YX]] | |||
[[Category: Cryle MJ]] | |||
[[Category: Ho YTC]] | |||
Latest revision as of 10:16, 21 November 2024
Non-ribosomal PCP-C didomain (ester stabilised leucine) acceptor bound stateNon-ribosomal PCP-C didomain (ester stabilised leucine) acceptor bound state
Structural highlights
FunctionPublication Abstract from PubMedNonribosomal peptide synthetases produce many important peptide natural products and are centred around carrier proteins (CPs) that deliver intermediates to various catalytic domains. We show that the replacement of CP substrate thioesters by stabilised ester analogues leads to active condensation domain complexes, whereas amide stabilisation generates non-functional complexes. Not always an innocent bystander: the impact of stabilised phosphopantetheine moieties when studying nonribosomal peptide biosynthesis.,Ho YTC, Kaczmarski JA, Tailhades J, Izore T, Steer DL, Schittenhelm RB, Tosin M, Jackson CJ, Cryle MJ Chem Commun (Camb). 2023 Jun 29;59(53):8234-8237. doi: 10.1039/d3cc01578e. PMID:37310188[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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