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==The crystal structure of CT mutant== | ==The crystal structure of CT mutant== | ||
<StructureSection load='5dlk' size='340' side='right' caption='[[5dlk]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5dlk' size='340' side='right'caption='[[5dlk]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dlk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DLK OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5dlk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_aethiopicum Penicillium aethiopicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DLK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5dlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dlk OCA], [https://pdbe.org/5dlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dlk RCSB], [https://www.ebi.ac.uk/pdbsum/5dlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dlk ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/F1CWE4_PENAE F1CWE4_PENAE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nonribosomal peptide synthetases (NRPSs) in fungi biosynthesize important pharmaceutical compounds, including penicillin, cyclosporine and echinocandin. To understand the fungal strategy of forging the macrocyclic peptide linkage, we determined the crystal structures of the terminal condensation-like (CT) domain and the holo thiolation (T)-CT complex of Penicillium aethiopicum TqaA. The first, to our knowledge, structural depiction of the terminal module in a fungal NRPS provides a molecular blueprint for generating new macrocyclic peptide natural products. | |||
Structural basis of nonribosomal peptide macrocyclization in fungi.,Zhang J, Liu N, Cacho RA, Gong Z, Liu Z, Qin W, Tang C, Tang Y, Zhou J Nat Chem Biol. 2016 Dec;12(12):1001-1003. doi: 10.1038/nchembio.2202. Epub 2016, Oct 17. PMID:27748753<ref>PMID:27748753</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5dlk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Penicillium aethiopicum]] | ||
[[Category: | [[Category: Tang Y]] | ||
[[Category: | [[Category: Zhang JR]] | ||
[[Category: | [[Category: Zhou JH]] | ||
Latest revision as of 00:48, 29 June 2023
The crystal structure of CT mutantThe crystal structure of CT mutant
Structural highlights
FunctionPublication Abstract from PubMedNonribosomal peptide synthetases (NRPSs) in fungi biosynthesize important pharmaceutical compounds, including penicillin, cyclosporine and echinocandin. To understand the fungal strategy of forging the macrocyclic peptide linkage, we determined the crystal structures of the terminal condensation-like (CT) domain and the holo thiolation (T)-CT complex of Penicillium aethiopicum TqaA. The first, to our knowledge, structural depiction of the terminal module in a fungal NRPS provides a molecular blueprint for generating new macrocyclic peptide natural products. Structural basis of nonribosomal peptide macrocyclization in fungi.,Zhang J, Liu N, Cacho RA, Gong Z, Liu Z, Qin W, Tang C, Tang Y, Zhou J Nat Chem Biol. 2016 Dec;12(12):1001-1003. doi: 10.1038/nchembio.2202. Epub 2016, Oct 17. PMID:27748753[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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