1sqg
From Proteopedia
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| - | [[Image:1sqg.gif|left|200px]] | + | [[Image:1sqg.gif|left|200px]] |
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| - | '''The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution''' | + | {{Structure |
| + | |PDB= 1sqg |SIZE=350|CAPTION= <scene name='initialview01'>1sqg</scene>, resolution 1.65Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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]) | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SQG is a [ | + | 1SQG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14656444 14656444] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rossmann-fold]] | [[Category: rossmann-fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:23 2008'' |
Revision as of 12:08, 20 March 2008
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| , resolution 1.65Å | |||||||
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| Gene: | SUN, FMU, FMV, RSMB, B3289 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of the E. coli Fmu apoenzyme at 1.65 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
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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