1ri4: Difference between revisions

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==Structure and mechanism of mRNA cap (guanine N-7) methyltransferase==
The line below this paragraph, containing "STRUCTURE_1ri4", creates the "Structure Box" on the page.
<StructureSection load='1ri4' size='340' side='right'caption='[[1ri4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ri4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RI4 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]] 2.4&#8491;</td></tr>
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<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_1ri4|  PDB=1ri4  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ri4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ri4 OCA], [https://pdbe.org/1ri4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ri4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ri4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ri4 ProSAT]</span></td></tr>
 
</table>
'''Structure and mechanism of mRNA cap (guanine N-7) methyltransferase'''
== Function ==
 
[https://www.uniprot.org/uniprot/MCES_ENCCU MCES_ENCCU] mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.<ref>PMID:15760890</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
A suite of crystal structures is reported for a cellular mRNA cap (guanine-N7) methyltransferase in complex with AdoMet, AdoHcy, and the cap guanylate. Superposition of ligand complexes suggests an in-line mechanism of methyl transfer, albeit without direct contacts between the enzyme and either the N7 atom of guanine (the attacking nucleophile), the methyl carbon of AdoMet, or the sulfur of AdoMet/AdoHcy (the leaving group). The structures indicate that catalysis of cap N7 methylation is accomplished by optimizing proximity and orientation of the substrates, assisted by a favorable electrostatic environment. The enzyme-ligand structures, together with new mutational data, fully account for the biochemical specificity of the cap guanine-N7 methylation reaction, an essential and defining step of eukaryotic mRNA synthesis.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1ri4_consurf.spt"</scriptWhenChecked>
1RI4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI4 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Structure and mechanism of mRNA cap (guanine-N7) methyltransferase., Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD, Mol Cell. 2004 Jan 16;13(1):77-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14731396 14731396]
</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=1ri4 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Encephalitozoon cuniculi]]
[[Category: Encephalitozoon cuniculi]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fabrega, C.]]
[[Category: Fabrega C]]
[[Category: Hausmann, S.]]
[[Category: Hausmann S]]
[[Category: Lima, C D.]]
[[Category: Lima CD]]
[[Category: Shen, V.]]
[[Category: Shen V]]
[[Category: Shuman, S.]]
[[Category: Shuman S]]
[[Category: Cap]]
[[Category: M7g]]
[[Category: Messenger rna cap]]
[[Category: Methyltransferase]]
[[Category: Rna]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:31:30 2008''

Latest revision as of 11:23, 14 February 2024

Structure and mechanism of mRNA cap (guanine N-7) methyltransferaseStructure and mechanism of mRNA cap (guanine N-7) methyltransferase

Structural highlights

1ri4 is a 1 chain structure with sequence from Encephalitozoon cuniculi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCES_ENCCU mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.[1]

Evolutionary Conservation

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

References

  1. Hausmann S, Zheng S, Fabrega C, Schneller SW, Lima CD, Shuman S. Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis. J Biol Chem. 2005 May 27;280(21):20404-12. Epub 2005 Mar 9. PMID:15760890 doi:10.1074/jbc.M501073200

1ri4, resolution 2.40Å

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