1ZJR

Crystal Structure of A. aeolicus TrmH/SpoU tRNA modifying enzyme

Summary for 1ZJR

• Entry DOI: 10.2210/pdb1zjr/pdb
• Descriptor: tRNA (Guanosine-2'-O-)-methyltransferase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: methylase, rna modifying enzyme, topological knot, transferase
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm (Potential): O67577
• Total number of polymer chains: 1
• Total formula weight: 24897.78

Authors

Pleshe, E.,Truesdell, J.,Batey, R.T. (deposition date: 2005-04-30, release date: 2005-08-09, Last modification date: 2023-08-23)

Primary citation

Pleshe, E.,Truesdell, J.,Batey, R.T.
Structure of a class II TrmH tRNA-modifying enzyme from Aquifex aeolicus.
Acta Crystallogr.,Sect.F, 61:722-728, 2005

PubMed Abstract: Biological RNAs contain a variety of post-transcriptional modifications that facilitate their efficient function in the cellular environment. One of the two most common forms of modification is methylation of the 2'-hydroxyl group of the ribose sugar, which is performed by a number of S-adenosylmethionine (SAM) dependent methyltransferases. In bacteria, many of these modifications in tRNA and rRNA are carried out by the alpha/beta-knot superfamily of enzymes, whose SAM-binding pocket is created by a characteristic deep trefoil knot. TrmH, an enzyme found throughout all three kingdoms of life, modifies the universally conserved guanosine 18 position of tRNA. The crystal structure of TrmH from the thermophilic bacterium Aquifex aeolicus has been determined at 1.85 A resolution using data collected from a synchrotron-radiation source. The protein reveals a fold typical of members of the SpoU clan of proteins, a subfamily of the alpha/beta-knot superfamily, with alpha-helical extensions at the N- and C-termini that are likely to be involved in tRNA binding.

PubMed: 16511140
DOI: 10.1107/S1744309105022980

Experimental method

X-RAY DIFFRACTION (1.85 Å)