2nyu: Difference between revisions

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


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==Crystal Structure of Human FtsJ homolog 2 (E.coli) protein in complex with S-adenosylmethionine==
The line below this paragraph, containing "STRUCTURE_2nyu", creates the "Structure Box" on the page.
<StructureSection load='2nyu' size='340' side='right'caption='[[2nyu]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
-->
<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>
{{STRUCTURE_2nyu|  PDB=2nyu  |  SCENE=  }}
<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>
 
</table>
===Crystal Structure of Human FtsJ homolog 2 (E.coli) protein in complex with S-adenosylmethionine===
== 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 ==
==About this Structure==
[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>
2NYU is a 2 chains structure of sequences 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].  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <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: Arrowsmith, C H.]]
[[Category: Large Structures]]
[[Category: Bochkarev, A.]]
[[Category: Arrowsmith CH]]
[[Category: Dong, A.]]
[[Category: Bochkarev A]]
[[Category: Edwards, A M.]]
[[Category: Dong A]]
[[Category: Loppnau, P.]]
[[Category: Edwards AM]]
[[Category: Plotnikov, A N.]]
[[Category: Loppnau P]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Plotnikov AN]]
[[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 Feb 16 21:49:42 2009''

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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