1sqf
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= SUN, FMU, FMV, RSMB, B3289 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= SUN, FMU, FMV, RSMB, B3289 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sqf|1SQF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqf OCA], [http://www.ebi.ac.uk/pdbsum/1sqf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sqf RCSB]</span> | ||
}} | }} | ||
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[[Category: Nunes, C R.]] | [[Category: Nunes, C R.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
| - | [[Category: SAM]] | ||
[[Category: methyltransferase-fold]] | [[Category: methyltransferase-fold]] | ||
[[Category: mixed beta sheet]] | [[Category: mixed beta sheet]] | ||
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[[Category: rossmann-fold]] | [[Category: rossmann-fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:37 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SUN, FMU, FMV, RSMB, B3289 (Escherichia coli) | ||||||
| Related: | 1SQF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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