1p9p

<table><tr><td colspan='2'>[[1p9p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P9P FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRMD OR B2607 OR C3128 OR Z3901 OR ECS3470 OR SF2667 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.221 and 2.1.1.228 2.1.1.221 and 2.1.1.228] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9p OCA], [http://pdbe.org/1p9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p9p RCSB], [http://www.ebi.ac.uk/pdbsum/1p9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9p ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TRMD_ECOLI TRMD_ECOLI]] Specifically methylates guanosine-37 in various tRNAs.<ref>PMID:14583191</ref>

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== Publication Abstract from PubMed ==

The crystal structure of Escherichia coli tRNA (guanosine-1) methyltransferase (TrmD) complexed with S-adenosyl homocysteine (AdoHcy) has been determined at 2.5A resolution. TrmD, which methylates G37 of tRNAs containing the sequence G36pG37, is a homo-dimer. Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain. The two bound AdoHcy moieties are buried at the bottom of deep clefts. The dimer structure appears integral to the formation of the catalytic center of the enzyme and this arrangement strongly suggests that the anticodon loop of tRNA fits into one of these clefts for methyl transfer to occur. In addition, adjacent hydrophobic sites in the cleft delineate a defined pocket, which may accommodate the GpG sequence during catalysis. The dimer contains two deep trefoil peptide knots and a peptide loop extending from each knot embraces the AdoHcy adenine ring. Mutational analyses demonstrate that the knot is important for AdoMet binding and catalytic activity, and that the C-terminal domain is not only required for tRNA binding but plays a functional role in catalytic activity.

Insights into catalysis by a knotted TrmD tRNA methyltransferase.,Elkins PA, Watts JM, Zalacain M, van Thiel A, Vitazka PR, Redlak M, Andraos-Selim C, Rastinejad F, Holmes WM J Mol Biol. 2003 Nov 7;333(5):931-49. PMID:14583191<ref>PMID:14583191</ref>

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

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<div class="pdbe-citations 1p9p" style="background-color:#fffaf0;"></div>

[[Category: Ecoli]]

[[Category: Andraos-Selim, C]]

[[Category: Elkins, P A]]

[[Category: Holmes, W M]]

[[Category: Rastinejad, F]]

[[Category: Redlak, M]]

[[Category: Thiel, A Van]]

[[Category: Vitaszka, P R]]

[[Category: Watts, J M]]

[[Category: Zalacain, M]]

[[Category: Spout]]