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[[Image:2nyu.gif|left|200px]]


{{Structure
==Crystal Structure of Human FtsJ homolog 2 (E.coli) protein in complex with S-adenosylmethionine==
|PDB= 2nyu |SIZE=350|CAPTION= <scene name='initialview01'>2nyu</scene>, resolution 1.76&Aring;
<StructureSection load='2nyu' size='340' side='right'caption='[[2nyu]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>
<table><tr><td colspan='2'>[[2nyu]] is a 2 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=2NYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NYU FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
|GENE= FTSJ2, FJH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyu OCA], [https://pdbe.org/2nyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nyu RCSB], [https://www.ebi.ac.uk/pdbsum/2nyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nyu ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyu OCA], [http://www.ebi.ac.uk/pdbsum/2nyu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nyu RCSB]</span>
== Disease ==
}}
[https://www.uniprot.org/uniprot/MRM2_HUMAN MRM2_HUMAN] The disease may be caused by variants affecting the gene represented in this entry.
 
== Function ==
'''Crystal Structure of Human FtsJ homolog 2 (E.coli) protein in complex with S-adenosylmethionine'''
[https://www.uniprot.org/uniprot/MRM2_HUMAN MRM2_HUMAN] S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.<ref>PMID:25009282</ref> <ref>PMID:25074936</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==About this Structure==
Check<jmol>
2NYU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYU OCA].  
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/2nyu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2nyu ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Bochkarev, A.]]
[[Category: Bochkarev A]]
[[Category: Dong, A.]]
[[Category: Dong A]]
[[Category: Edwards, A M.]]
[[Category: Edwards AM]]
[[Category: Loppnau, P.]]
[[Category: Loppnau P]]
[[Category: Plotnikov, A N.]]
[[Category: Plotnikov AN]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M.]]
[[Category: Weigelt J]]
[[Category: Weigelt, J.]]
[[Category: Wu H]]
[[Category: Wu, H.]]
[[Category: Zeng H]]
[[Category: Zeng, H.]]
[[Category: ribosomal rna]]
[[Category: sam]]
[[Category: sgc]]
[[Category: structural genomic]]
[[Category: structural genomics consortium]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:10:25 2008''

Latest revision as of 13:27, 30 August 2023

Crystal Structure of Human FtsJ homolog 2 (E.coli) protein in complex with S-adenosylmethionineCrystal Structure of Human FtsJ homolog 2 (E.coli) protein in complex with S-adenosylmethionine

Structural highlights

2nyu is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.76Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MRM2_HUMAN The disease may be caused by variants affecting the gene represented in this entry.

Function

MRM2_HUMAN S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Rorbach J, Boesch P, Gammage PA, Nicholls TJ, Pearce SF, Patel D, Hauser A, Perocchi F, Minczuk M. MRM2 and MRM3 are involved in biogenesis of the large subunit of the mitochondrial ribosome. Mol Biol Cell. 2014 Sep 1;25(17):2542-55. PMID:25009282 doi:10.1091/mbc.E14-01-0014
  2. ↑ Lee KW, Bogenhagen DF. Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA). J Biol Chem. 2014 Sep 5;289(36):24936-42. PMID:25074936 doi:10.1074/jbc.C114.581868

2nyu, resolution 1.76Å

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