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| '''Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition'''
| | ===Crystal structure of tRNA(m1G37)methyltransferase: Insight into tRNA recognition=== |
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| ==Overview==
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| tRNA(m(1)G37)methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L- methionine (AdoMet) to G(37) within a subset of bacterial tRNA species, which have a G residue at the 36th position. The modified guanosine is adjacent to and 3' of the anticodon and is essential for the maintenance of the correct reading frame during translation. Here we report four crystal structures of TrmD from Haemophilus influenzae, as binary complexes with either AdoMet or S-adenosyl-L-homocysteine (AdoHcy), as a ternary complex with AdoHcy and phosphate, and as an apo form. This first structure of TrmD indicates that it functions as a dimer. It also suggests the binding mode of G(36)G(37) in the active site of TrmD and the catalytic mechanism. The N-terminal domain has a trefoil knot, in which AdoMet or AdoHcy is bound in a novel, bent conformation. The C-terminal domain shows structural similarity to trp repressor. We propose a plausible model for the TrmD(2)-tRNA(2) complex, which provides insights into recognition of the general tRNA structure by TrmD.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12773376}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12773376 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12773376}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Trmd]] | | [[Category: Trmd]] |
| [[Category: Trna modification]] | | [[Category: Trna modification]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:58:14 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:25:51 2008'' |
