2fca

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{{STRUCTURE_2fca| PDB=2fca | SCENE= }}
{{STRUCTURE_2fca| PDB=2fca | SCENE= }}
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'''The structure of BsTrmB'''
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===The structure of BsTrmB===
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==Overview==
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The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46) methyltransferase, was determined at a resolution of 2.1 A. 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.
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{{ABSTRACT_PUBMED_16600901}}
==About this Structure==
==About this Structure==
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[[Category: Zegers, I.]]
[[Category: Zegers, I.]]
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:56:54 2008''

Revision as of 12:56, 27 July 2008

Image:2fca.png

Template:STRUCTURE 2fca

The structure of BsTrmB

Template:ABSTRACT PUBMED 16600901

About this Structure

2FCA is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase., Zegers I, Gigot D, van Vliet F, Tricot C, Aymerich S, Bujnicki JM, Kosinski J, Droogmans L, Nucleic Acids Res. 2006 Apr 5;34(6):1925-34. Print 2006. PMID:16600901

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