1fmt
From Proteopedia
(New page: 200px<br /><applet load="1fmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmt, resolution 2.0Å" /> '''METHIONYL-TRNAFMET FO...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fmt.gif|left|200px]]<br /><applet load="1fmt" size=" | + | [[Image:1fmt.gif|left|200px]]<br /><applet load="1fmt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fmt, resolution 2.0Å" /> | caption="1fmt, resolution 2.0Å" /> | ||
'''METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI'''<br /> | '''METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Formylation of the methionyl moiety esterified to the 3' end of tRNA(f)Met | + | Formylation of the methionyl moiety esterified to the 3' end of tRNA(f)Met is a key step in the targeting of initiator tRNA towards the translation start machinery in prokaryotes. Accordingly, the presence of methionyl-tRNA(f)Met formyltransferase (FMT), the enzyme responsible for this formylation, is necessary for the normal growth of Escherichia coli. The present work describes the structure of crystalline E.coli FMT at 2.0 A, resolution. The protein has an N-terminal domain containing a Rossmann fold. This domain closely resembles that of the glycinamide ribonucleotide formyltransferase (GARF), an enzyme which, like FMT, uses N-10 formyltetrahydrofolate as formyl donor. However, FMT can be distinguished from GARF by a flexible loop inserted within its Rossmann fold. In addition, FMT possesses a C-terminal domain with a beta-barrel reminiscent of an OB fold. This latter domain provides a positively charged side oriented towards the active site. Biochemical evidence is presented for the involvement of these two idiosyncratic regions (the flexible loop in the N-terminal domain, and the C-terminal domain) in the binding of the tRNA substrate. |
==About this Structure== | ==About this Structure== | ||
| - | 1FMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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:// | + | 1FMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1FMT OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: translation initiation]] | [[Category: translation initiation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:24 2008'' |
Revision as of 10:40, 21 February 2008
|
METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI
Overview
Formylation of the methionyl moiety esterified to the 3' end of tRNA(f)Met is a key step in the targeting of initiator tRNA towards the translation start machinery in prokaryotes. Accordingly, the presence of methionyl-tRNA(f)Met formyltransferase (FMT), the enzyme responsible for this formylation, is necessary for the normal growth of Escherichia coli. The present work describes the structure of crystalline E.coli FMT at 2.0 A, resolution. The protein has an N-terminal domain containing a Rossmann fold. This domain closely resembles that of the glycinamide ribonucleotide formyltransferase (GARF), an enzyme which, like FMT, uses N-10 formyltetrahydrofolate as formyl donor. However, FMT can be distinguished from GARF by a flexible loop inserted within its Rossmann fold. In addition, FMT possesses a C-terminal domain with a beta-barrel reminiscent of an OB fold. This latter domain provides a positively charged side oriented towards the active site. Biochemical evidence is presented for the involvement of these two idiosyncratic regions (the flexible loop in the N-terminal domain, and the C-terminal domain) in the binding of the tRNA substrate.
About this Structure
1FMT is a Single protein structure of sequence from Escherichia coli. Active as Methionyl-tRNA formyltransferase, with EC number 2.1.2.9 Full crystallographic information is available from OCA.
Reference
Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase., Schmitt E, Blanquet S, Mechulam Y, EMBO J. 1996 Sep 2;15(17):4749-58. PMID:8887566
Page seeded by OCA on Thu Feb 21 12:40:24 2008
