1SQF

The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution

Summary for 1SQF

• Entry DOI: 10.2210/pdb1sqf/pdb
• Related: 1SQF
• Descriptor: SUN protein, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: rossmann-fold, mixed beta sheet, methyltransferase-fold, rna-binding domain, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Potential): P36929
• Total number of polymer chains: 1
• Total formula weight: 48806.82

Authors

Foster, P.G.,Nunes, C.R.,Greene, P.,Moustakas, D.,Stroud, R.M. (deposition date: 2004-03-18, release date: 2004-05-18, Last modification date: 2024-02-14)

Primary citation

Foster, P.G.,Nunes, C.R.,Greene, P.,Moustakas, D.,Stroud, R.M.
The First Structure of an RNA m5C Methyltransferase, Fmu, Provides Insight into Catalytic Mechanism and Specific Binding of RNA Substrate
Structure, 11:1609-1620, 2003

PubMed Abstract: 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.

PubMed: 14656444
DOI: 10.1016/j.str.2003.10.014

Experimental method

X-RAY DIFFRACTION (2.1 Å)