OpenAccessBelV2, France, Analysis, bibRecord, 000169

Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase

Identifieur interne : 000169 ( France/Analysis ); précédent : 000168; suivant : 000170

Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase

Auteurs : Ingrid Zegers ; Daniel Gigot [Belgique] ; Franc Oise Van Vliet [Belgique] ; Catherine Tricot [Belgique] ; Ste Phane Aymerich [France] ; Janusz M. Bujnicki [Pologne, Belgique] ; Jan Kosinski [Pologne] ; Louis Droogmans [Belgique]

Source :

Nucleic Acids Research [ 0305-1048 ] ; 2006.

RBID : ISTEX:3ED1F78ABEAD7E85A7942302868BC4BCDACF5BE9

Abstract

The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46) methyltransferase, was determined at a resolution of 2.1 Å. This is the first structure of a member of the TrmB family to be determined by X-ray crystallography. It reveals a unique variant of the Rossmann-fold methyltransferase (RFM) structure, with the N-terminal helix folded on the opposite site of the catalytic domain. The architecture of the active site and a computational docking model of BsTrmB in complex with the methyl group donor S-adenosyl-l-methionine and the tRNA substrate provide an explanation for results from mutagenesis studies of an orthologous enzyme from Escherichia coli (EcTrmB). However, unlike EcTrmB, BsTrmB is shown here to be dimeric both in the crystal and in solution. The dimer interface has a hydrophobic core and buries a potassium ion and five water molecules. The evolutionary analysis of the putative interface residues in the TrmB family suggests that homodimerization may be a specific feature of TrmBs from Bacilli, which may represent an early stage of evolution to an obligatory dimer.

Url:

https://api.istex.fr/document/3ED1F78ABEAD7E85A7942302868BC4BCDACF5BE9/fulltext/pdf

DOI: 10.1093/nar/gkl116

Affiliations:

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ISTEX:3ED1F78ABEAD7E85A7942302868BC4BCDACF5BE9

Le document en format XML

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<front><div type="abstract" xml:lang="en">The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46) methyltransferase, was determined at a resolution of 2.1 Å. This is the first structure of a member of the TrmB family to be determined by X-ray crystallography. It reveals a unique variant of the Rossmann-fold methyltransferase (RFM) structure, with the N-terminal helix folded on the opposite site of the catalytic domain. The architecture of the active site and a computational docking model of BsTrmB in complex with the methyl group donor S-adenosyl-l-methionine and the tRNA substrate provide an explanation for results from mutagenesis studies of an orthologous enzyme from Escherichia coli (EcTrmB). However, unlike EcTrmB, BsTrmB is shown here to be dimeric both in the crystal and in solution. The dimer interface has a hydrophobic core and buries a potassium ion and five water molecules. The evolutionary analysis of the putative interface residues in the TrmB family suggests that homodimerization may be a specific feature of TrmBs from Bacilli, which may represent an early stage of evolution to an obligatory dimer.</div>
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Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase

Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase

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Abstract

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