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3epk

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Template:STRUCTURE 3epk

Contents

CRYSTALLOGRAPHIC SNAPSHOTS OF EUKARYOTIC DIMETHYLALLYLTRANSFERASE ACTING ON TRNA: INSIGHT INTO TRNA RECOGNITION AND REACTION MECHANISM

Template:ABSTRACT PUBMED 18852462

Function

[MOD5_YEAST] Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in the anticodon loop on a specific subset of tRNAs both in the cytosol and the mitochondrion, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). This modification optimizes the codon:anticodon fit in the ribosome and promotes translational fidelity. Competes with the farnesyl pyrophosphate synthase ERG20 for the common substrate dimethylallyl diphosphate (DMAPP).[1] [2] [3]

About this Structure

3epk is a 4 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA.

Reference

  • Zhou C, Huang RH. Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism. Proc Natl Acad Sci U S A. 2008 Oct 21;105(42):16142-7. Epub 2008 Oct 13. PMID:18852462
  1. ↑ Dihanich ME, Najarian D, Clark R, Gillman EC, Martin NC, Hopper AK. Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae. Mol Cell Biol. 1987 Jan;7(1):177-84. PMID:3031456
  2. ↑ Benko AL, Vaduva G, Martin NC, Hopper AK. Competition between a sterol biosynthetic enzyme and tRNA modification in addition to changes in the protein synthesis machinery causes altered nonsense suppression. Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):61-6. PMID:10618371
  3. ↑ Lamichhane TN, Blewett NH, Maraia RJ. Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases. RNA. 2011 Oct;17(10):1846-57. doi: 10.1261/rna.2628611. Epub 2011 Aug 26. PMID:21873461 doi:http://dx.doi.org/10.1261/rna.2628611

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