3axz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Haemophilus influenzae TrmD in complex with adenosine== | |
| + | <StructureSection load='3axz' size='340' side='right'caption='[[3axz]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3axz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AXZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3axz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axz OCA], [https://pdbe.org/3axz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3axz RCSB], [https://www.ebi.ac.uk/pdbsum/3axz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3axz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRMD_HAEIN TRMD_HAEIN] Specifically methylates guanosine-37 in various tRNAs (By similarity).[HAMAP-Rule:MF_00605] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N(1) of G37, using catalytic motifs that share no sequence or structural homology. Here we show that natural and synthetic analogs of AdoMet are unable to distinguish TrmD from Trm5. Instead, fragments of AdoMet, adenosine and methionine, are selectively inhibitory of TrmD rather than Trm5. Detailed structural information of the two enzymes in complex with adenosine reveals how Trm5 escapes targeting by adopting an altered structure, whereas TrmD is trapped by targeting due to its rigid structure that stably accommodates the fragment. Free energy analysis exposes energetic disparities between the two enzymes in how they approach the binding of AdoMet versus fragments and provides insights into the design of inhibitors selective for TrmD. | ||
| - | + | Differentiating analogous tRNA methyltransferases by fragments of the methyl donor.,Lahoud G, Goto-Ito S, Yoshida K, Ito T, Yokoyama S, Hou YM RNA. 2011 Jul;17(7):1236-46. Epub 2011 May 20. PMID:21602303<ref>PMID:21602303</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3axz" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Haemophilus influenzae Rd KW20]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Goto-Ito S]] | ||
| + | [[Category: Hou YM]] | ||
| + | [[Category: Ito T]] | ||
| + | [[Category: Yokoyama S]] | ||
| + | [[Category: Yoshida K]] | ||
Current revision
Crystal structure of Haemophilus influenzae TrmD in complex with adenosine
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