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<StructureSection load='7kw2' size='340' side='right'caption='[[7kw2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='7kw2' size='340' side='right'caption='[[7kw2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7kw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thefy Thefy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KW2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7kw2]] 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=7KW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KW2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr>
</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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tfu_1867 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</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=7kw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kw2 OCA], [https://pdbe.org/7kw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kw2 RCSB], [https://www.ebi.ac.uk/pdbsum/7kw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kw2 ProSAT]</span></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=7kw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kw2 OCA], [https://pdbe.org/7kw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kw2 RCSB], [https://www.ebi.ac.uk/pdbsum/7kw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kw2 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q47NR9_THEFY Q47NR9_THEFY]
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains.
 
Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.,Izore T, Candace Ho YT, Kaczmarski JA, Gavriilidou A, Chow KH, Steer DL, Goode RJA, Schittenhelm RB, Tailhades J, Tosin M, Challis GL, Krenske EH, Ziemert N, Jackson CJ, Cryle MJ Nat Commun. 2021 May 4;12(1):2511. doi: 10.1038/s41467-021-22623-0. PMID:33947858<ref>PMID:33947858</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kw2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thefy]]
[[Category: Thermobifida fusca YX]]
[[Category: Challis, G L]]
[[Category: Challis GL]]
[[Category: Chow, K H]]
[[Category: Chow KH]]
[[Category: Cryle, M J]]
[[Category: Cryle MJ]]
[[Category: Gavriilidou, A]]
[[Category: Gavriilidou A]]
[[Category: Goode, R J.A]]
[[Category: Goode RJA]]
[[Category: Ho, Y T.C]]
[[Category: Ho YTC]]
[[Category: Izore, T]]
[[Category: Izore T]]
[[Category: Jackson, C J]]
[[Category: Jackson CJ]]
[[Category: Kaczmarski, J A]]
[[Category: Kaczmarski JA]]
[[Category: Krenske, E H]]
[[Category: Krenske EH]]
[[Category: Schittenhelm, R B]]
[[Category: Schittenhelm RB]]
[[Category: Steer, D]]
[[Category: Steer D]]
[[Category: Tailhades, J]]
[[Category: Tailhades J]]
[[Category: Tosin, M]]
[[Category: Tosin M]]
[[Category: Ziemert, N]]
[[Category: Ziemert N]]
[[Category: Biosynthetic protein]]
[[Category: C-domain]]
[[Category: Nrp]]
[[Category: Pcp-domain]]

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