5dij

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Current revision (09:09, 20 March 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/F1CWE4_PENAE F1CWE4_PENAE]
[https://www.uniprot.org/uniprot/F1CWE4_PENAE F1CWE4_PENAE]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 5dij" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

The crystal structure of CT

PDB ID 5dij

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