5inj: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A182DWE5_9ACTN A0A182DWE5_9ACTN]  
[https://www.uniprot.org/uniprot/A0A182DWE5_9ACTN A0A182DWE5_9ACTN]  
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== Publication Abstract from PubMed ==
This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug.


Structure and specificity of a permissive bacterial C-prenyltransferase.,Elshahawi SI, Cao H, Shaaban KA, Ponomareva LV, Subramanian T, Farman ML, Spielmann HP, Phillips GN Jr, Thorson JS, Singh S Nat Chem Biol. 2017 Feb 6. doi: 10.1038/nchembio.2285. PMID:28166207<ref>PMID:28166207</ref>
==See Also==
 
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
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</StructureSection>
</StructureSection>

Latest revision as of 12:34, 6 March 2024

Crystal Structure of Prenyltransferase PriB Ternary Complex with L-Tryptophan and Dimethylallyl thiolodiphosphate (DMSPP)

5inj, resolution 1.40Å

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