3ay0 | pdb_00003ay0

Crystal structure of Methanocaldococcus jannaschii Trm5 in complex with adenosine

spinqualitylabelsall models 3ay0, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ay0 is a 2 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.05Å Ligands: ADN, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRM5B_METJA Specifically methylates the N1 position of guanosine-37 in various tRNAs. Publication Abstract from PubMed Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N(1) of G37, using catalytic motifs that share no sequence or structural homology. Here we show that natural and synthetic analogs of AdoMet are unable to distinguish TrmD from Trm5. Instead, fragments of AdoMet, adenosine and methionine, are selectively inhibitory of TrmD rather than Trm5. Detailed structural information of the two enzymes in complex with adenosine reveals how Trm5 escapes targeting by adopting an altered structure, whereas TrmD is trapped by targeting due to its rigid structure that stably accommodates the fragment. Free energy analysis exposes energetic disparities between the two enzymes in how they approach the binding of AdoMet versus fragments and provides insights into the design of inhibitors selective for TrmD. Differentiating analogous tRNA methyltransferases by fragments of the methyl donor.,Lahoud G, Goto-Ito S, Yoshida K, Ito T, Yokoyama S, Hou YM RNA. 2011 Jul;17(7):1236-46. Epub 2011 May 20. PMID:21602303 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TRNA methyltransferase 3D structures

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