5nfj: Difference between revisions
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<StructureSection load='5nfj' size='340' side='right'caption='[[5nfj]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='5nfj' size='340' side='right'caption='[[5nfj]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nfj]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5nfj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NFJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nfj OCA], [https://pdbe.org/5nfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nfj RCSB], [https://www.ebi.ac.uk/pdbsum/5nfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nfj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/TM10C_HUMAN TM10C_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TM10C_HUMAN TM10C_HUMAN] Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation (PubMed:18984158, PubMed:21593607, PubMed:23042678, PubMed:27132592). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158). Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit (PubMed:23042678). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA (PubMed:29072297).<ref>PMID:18984158</ref> <ref>PMID:21593607</ref> <ref>PMID:23042678</ref> <ref>PMID:27132592</ref> <ref>PMID:29040705</ref> <ref>PMID:29072297</ref> | ||
==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith C]] | ||
[[Category: Bountra | [[Category: Bountra C]] | ||
[[Category: Burgess-Brown | [[Category: Burgess-Brown N]] | ||
[[Category: Chalk | [[Category: Chalk R]] | ||
[[Category: Edwards C]] | |||
[[Category: Edwards | [[Category: Fairhead M]] | ||
[[Category: Fairhead | [[Category: Fitzpatrick F]] | ||
[[Category: Fitzpatrick | [[Category: Kopec J]] | ||
[[Category: Kopec | [[Category: Newman JA]] | ||
[[Category: Newman | [[Category: Oerum S]] | ||
[[Category: Oerum | [[Category: Oppermann U]] | ||
[[Category: Oppermann | [[Category: Shrestha L]] | ||
[[Category: Talon R]] | |||
[[Category: Shrestha | [[Category: Yue WW]] | ||
[[Category: Talon | [[Category: Von Delft F]] | ||
[[Category: Yue | |||
[[Category: | |||
Latest revision as of 12:53, 15 November 2023
Crystal structure of the methyltransferase subunit of human mitochondrial Ribonuclease P (MRPP1) bound to S-adenosyl-methionine (SAM)
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