1sqf

<StructureSection load='1sqf' size='340' side='right' caption='[[1sqf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sqf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SQF FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUN, FMU, FMV, RSMB, B3289 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1sqf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sqf RCSB], [http://www.ebi.ac.uk/pdbsum/1sqf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqf ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RSMB_ECOLI RSMB_ECOLI]] Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.<ref>PMID:10194318</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:14656444</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1sqf" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Foster, P G]]

[[Category: Greene, P]]

[[Category: Moustakas, D]]

[[Category: Nunes, C R]]

[[Category: Stroud, R M]]

[[Category: Transferase]]