4g5g
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/EFTU1_ECOLI EFTU1_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118] | [https://www.uniprot.org/uniprot/EFTU1_ECOLI EFTU1_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Synthetic studies of the antimicrobial secondary metabolite thiomuracin A (1) were initiated to improve chemical stability and physicochemical properties. Functional group modifications of 1 included removing the C2-C7 side chain, derivatizing the C84 epoxide region, and altering the C44 hydroxyphenylalanine motif. The resulting derivatives simplified and stabilized the chemical structure and were evaluated for antibacterial activity relative to 1. The simplified structure and improved organic solubility of the derivatives facilitated isolation yields from fermentation broths and simplified the procedures involved for the process. These advancements increased material supply for continued medicinal chemistry optimization and culminated in the identification of 2, a structurally simplified and chemically stable analogue of 1 which retained potent antibiotic activity. | ||
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| - | Antibiotic optimization and chemical structure stabilization of thiomuracin A.,LaMarche MJ, Leeds JA, Dzink-Fox J, Gangl E, Krastel P, Neckermann G, Palestrant D, Patane MA, Rann EM, Tiamfook S, Yu D J Med Chem. 2012 Aug 9;55(15):6934-41. doi: 10.1021/jm300783c. Epub 2012 Jul 31. PMID:22812377<ref>PMID:22812377</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4g5g" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Elongation factor 3D structures|Elongation factor 3D structures]] | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
ef-tu (Escherichia coli) complexed with nvp-ldu796
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