1sqg

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[[Image:1sqg.gif|left|200px]]<br /><applet load="1sqg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sqg, resolution 1.65&Aring;" />
 
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'''The crystal structure of the E. coli Fmu apoenzyme at 1.65 A resolution'''<br />
 
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==Overview==
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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 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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<StructureSection load='1sqg' size='340' side='right'caption='[[1sqg]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sqg]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQG FirstGlance]. <br>
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1SQG is a [http://en.wikipedia.org/wiki/Single_protein 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].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqg OCA], [https://pdbe.org/1sqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqg RCSB], [https://www.ebi.ac.uk/pdbsum/1sqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqg ProSAT]</span></td></tr>
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==Reference==
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</table>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14656444 14656444]
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== Function ==
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[https://www.uniprot.org/uniprot/RSMB_ECOLI RSMB_ECOLI] Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.<ref>PMID:10194318</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sq/1sqg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sqg ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Foster, P G.]]
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[[Category: Foster PG]]
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[[Category: Greene, P.]]
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[[Category: Greene P]]
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[[Category: Moustakas, D.]]
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[[Category: Moustakas D]]
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[[Category: Nunes, C R.]]
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[[Category: Nunes CR]]
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[[Category: Stroud, R M.]]
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[[Category: Stroud RM]]
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[[Category: methyltransferase-fold]]
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[[Category: mixed beta sheet]]
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[[Category: rna-binding domain]]
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[[Category: rossmann-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:08 2008''
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Current revision

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

PDB ID 1sqg

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OCA

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