2fmt

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(New page: 200px<br /><applet load="2fmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fmt, resolution 2.8&Aring;" /> '''METHIONYL-TRNAFMET FO...)
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'''METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET'''<br />
'''METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET'''<br />
==Overview==
==Overview==
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The crystal structure of Escherichia coli methionyl-tRNAfMet, transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8, A resolution. The formylation reaction catalyzed by this enzyme, irreversibly commits methionyl-tRNAfMet to initiation of translation in, eubacteria. In the three-dimensional model, the methionyl-tRNAfMet, formyltransferase fills in the inside of the L-shaped tRNA molecule on the, D-stem side. The anticodon stem and loop are away from the protein. An, enzyme loop is wedged in the major groove of the acceptor helix. As a, result, the C1-A72 mismatch characteristic of the initiator tRNA is split, and the 3' arm bends inside the active centre. This recognition mechanism, is markedly distinct from that of elongation factor Tu, which binds the, acceptor arm of aminoacylated elongator tRNAs on the T-stem side.
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The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet formyltransferase fills in the inside of the L-shaped tRNA molecule on the D-stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1-A72 mismatch characteristic of the initiator tRNA is split and the 3' arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T-stem side.
==About this Structure==
==About this Structure==
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2FMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and FME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methionyl-tRNA_formyltransferase Methionyl-tRNA formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.9 2.1.2.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FMT OCA].
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2FMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=FME:'>FME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methionyl-tRNA_formyltransferase Methionyl-tRNA formyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.9 2.1.2.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMT OCA].
==Reference==
==Reference==
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[[Category: initiation of translation]]
[[Category: initiation of translation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:38:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:01 2008''

Revision as of 15:23, 21 February 2008


2fmt, resolution 2.8Å

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METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET

Overview

The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet formyltransferase fills in the inside of the L-shaped tRNA molecule on the D-stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1-A72 mismatch characteristic of the initiator tRNA is split and the 3' arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T-stem side.

About this Structure

2FMT is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Methionyl-tRNA formyltransferase, with EC number 2.1.2.9 Full crystallographic information is available from OCA.

Reference

Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet., Schmitt E, Panvert M, Blanquet S, Mechulam Y, EMBO J. 1998 Dec 1;17(23):6819-26. PMID:9843487

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