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1sqg

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{{STRUCTURE_1sqg| PDB=1sqg | SCENE= }}
{{STRUCTURE_1sqg| PDB=1sqg | SCENE= }}
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'''The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution'''
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===The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14656444 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14656444}}
==About this Structure==
==About this Structure==
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[[Category: Rna-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:03:40 2008''

Revision as of 06:03, 29 July 2008

Image:1sqg.png

Template:STRUCTURE 1sqg

The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution

Template:ABSTRACT PUBMED 14656444

About this Structure

1SQG is a Single protein structure of sequence from Escherichia coli. 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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