1sqf
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(New page: 200px<br /><applet load="1sqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sqf, resolution 2.10Å" /> '''The crystal structur...)
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Revision as of 00:26, 21 November 2007
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The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution
Overview
The crystal structure of E. coli Fmu, determined at 1.65 A resolution for, the apoenzyme and 2.1 A resolution in complex with AdoMet, is the first, representative of the 5-methylcytosine RNA methyltransferase family that, includes the human nucleolar proliferation-associated protein p120. Fmu, contains three subdomains which share structural homology to DNA m(5)C, methyltransferases and two RNA binding protein families. In the binary, complex, the AdoMet cofactor is positioned within the active site near a, novel arrangement of two conserved cysteines that function in cytosine, methylation. The site is surrounded by a positively charged cleft large, enough to bind its unique target stem loop within 16S rRNA. Docking of, this stem loop RNA into the structure followed by molecular mechanics, shows that the Fmu structure is consistent with binding to the folded RNA, substrate.
About this Structure
1SQF is a Single protein structure of sequence from Escherichia coli with SAM as ligand. Full crystallographic information is available from OCA.
Reference
The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate., Foster PG, Nunes CR, Greene P, Moustakas D, Stroud RM, Structure. 2003 Dec;11(12):1609-20. PMID:14656444
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