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 2.10&Aring;" /> '''The crystal structur...)
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[[Image:1sqf.gif|left|200px]]<br /><applet load="1sqf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sqf.gif|left|200px]]<br /><applet load="1sqf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sqf, resolution 2.10&Aring;" />
caption="1sqf, resolution 2.10&Aring;" />
'''The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution'''<br />
'''The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution'''<br />
==Overview==
==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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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==
==About this Structure==
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1SQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SQF OCA].
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1SQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQF OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Foster, P.G.]]
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[[Category: Foster, P G.]]
[[Category: Greene, P.]]
[[Category: Greene, P.]]
[[Category: Moustakas, D.]]
[[Category: Moustakas, D.]]
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[[Category: Nunes, C.R.]]
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[[Category: Nunes, C R.]]
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[[Category: Stroud, R.M.]]
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[[Category: Stroud, R M.]]
[[Category: SAM]]
[[Category: SAM]]
[[Category: methyltransferase-fold]]
[[Category: methyltransferase-fold]]
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[[Category: rossmann-fold]]
[[Category: rossmann-fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:34:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:07 2008''

Revision as of 13:04, 21 February 2008


1sqf, resolution 2.10Å

Drag the structure with the mouse to rotate

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 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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