Modomics - A Database of RNA Modifications

ID Card:

Full name: N6-adenosine-methyltransferase non-catalytic subunit
Synonym: KIAA1627
GI: 24308265
COG: COG4725
UniProt: Q9HCE5
Structures: | 5IL1 | 5IL2 | 5K7M | 5K7U | 5K7W | 5L6D | 5L6E | 5TEY | 6TTP | 6TTT | 6TTV | 6TTW | 6TTX | 6TU1 | 6Y4G | 7ACD | 7NHG | 7NHH | 7NHI | 7NHJ | 7NHV | 7NI7 | 7NI8 | 7NI9 | 7NIA | 7NID | 7O08 | 7O09 | 7O0L | 7O0M | 7O0P | 7O0Q | 7O0R | 7O27 | 7O28 | 7O29 | 7O2E | 7O2F | 7O2H | 7O2I | 7O2X | 7OED | 7OEE | 7OEF | 7OEG | 7OEH | 7OEI | 7OEJ | 7OEK | 7OEL | 7OEM | 7OQL | 7OQO | 7OQP |
Alpha Fold Predicted Structure: AF-Q9HCE5-F1
Complex: METTL3-METTL14
Enzyme type: methyltransferase
Position of modification - modification: m:many - m6A


PDB Structures:


5IL1

Structure Description:

Title: Crystal structural of the METTL3-METTL14 complex for N6-adenosine methylation
Classification: RNA BINDING PROTEIN
Technique: X-Ray Diffraction
Resolution: 1.88
R value free: 0.205
R value observed: 0.176
R value work: 0.175

Abstract of the PDB Structure's related Publication:

Chemical modifications of RNA have essential roles in a vast range of cellular processes. N(6)-methyladenosine (m(6)A) is an abundant internal modification in messenger RNA and long non-coding RNA that can be dynamically added and removed by RNA methyltransferases (MTases) and demethylases, respectively. An MTase complex comprising methyltransferase-like 3 (METTL3) and methyltransferase-like 14 (METTL14) efficiently catalyses methyl group transfer. In contrast to the well-studied DNA MTase, the exact roles of these two RNA MTases in the complex remain to be elucidated. Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 Å, respectively. Both METTL3 and METTL14 adopt a class I MTase fold and they interact with each other via an extensive hydrogen bonding network, generating a positively charged groove. Notably, AdoMet was observed in only the METTL3 pocket and not in METTL14. Combined with biochemical analysis, these results suggest that in the m(6)A MTase complex, METTL3 primarily functions as the catalytic core, while METTL14 serves as an RNA-binding platform, reminiscent of the target recognition domain of DNA N(6)-adenine MTase. This structural information provides an important framework for the functional investigation of m(6)A.

Download RCSB-PDB Structures:

Pdb Files   5IL0.pdb   5IL1.pdb   5IL2.pdb   5K7M.pdb   5K7U.pdb   5K7W.pdb   5L6D.pdb   5L6E.pdb   5TEY.pdb   6TTP.pdb   6TTT.pdb   6TTV.pdb   6TTW.pdb   6TTX.pdb   6TU1.pdb   6Y4G.pdb   7ACD.pdb   7NHG.pdb   7NHH.pdb   7NHI.pdb   7NHJ.pdb   7NHV.pdb   7NI7.pdb   7NI8.pdb   7NI9.pdb   7NIA.pdb   7NID.pdb   7O08.pdb   7O09.pdb   7O0L.pdb   7O0M.pdb   7O0P.pdb   7O0Q.pdb   7O0R.pdb   7O27.pdb   7O28.pdb   7O29.pdb   7O2E.pdb   7O2F.pdb   7O2H.pdb   7O2I.pdb   7O2X.pdb   7OED.pdb   7OEE.pdb   7OEF.pdb   7OEG.pdb   7OEH.pdb   7OEI.pdb   7OEJ.pdb   7OEK.pdb   7OEL.pdb   7OEM.pdb   7OQL.pdb   7OQO.pdb   7OQP.pdb  
Pdbx/mmCIF Files   5IL0.cif   5IL1.cif   5IL2.cif   5K7M.cif   5K7U.cif   5K7W.cif   5L6D.cif   5L6E.cif   5TEY.cif   6TTP.cif   6TTT.cif   6TTV.cif   6TTW.cif   6TTX.cif   6TU1.cif   6Y4G.cif   7ACD.cif   7NHG.cif   7NHH.cif   7NHI.cif   7NHJ.cif   7NHV.cif   7NI7.cif   7NI8.cif   7NI9.cif   7NIA.cif   7NID.cif   7O08.cif   7O09.cif   7O0L.cif   7O0M.cif   7O0P.cif   7O0Q.cif   7O0R.cif   7O27.cif   7O28.cif   7O29.cif   7O2E.cif   7O2F.cif   7O2H.cif   7O2I.cif   7O2X.cif   7OED.cif   7OEE.cif   7OEF.cif   7OEG.cif   7OEH.cif   7OEI.cif   7OEJ.cif   7OEK.cif   7OEL.cif   7OEM.cif   7OQL.cif   7OQO.cif   7OQP.cif  


Protein sequence:

MDSRLQEIRERQKLRRQLLAQQLGAESADSIGAVLNSKDEQREIAETRETCRASYDTSAPNAKRKYLDEGETDEDKMEEYKDELEMQQDEENLPYEEEIYKDSSTFLKGTQSLNPHNDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLEEYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLDPKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPGWLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERLRPKSPPPKSKSDRGGGAPRGGGRGGTSAGRGRERNRSNFRGERGGFRGGRGGAHRGGFPPR

Comments:

METTL14 is a methyltransferase which forms a stable heterodimer with METTL3. The complex mediates m6A deposition on nuclear RNA.





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M D S R L Q E I R E R Q K L R R Q L L A Q Q L G A E S A D S I G A V L N S K D E Q R E I A E T R E T C R A S Y D T S A P N A K R K Y L D E G E T D E D K M E E Y K D E L E M Q Q D E E N L P Y E E E I Y K D S S T F L K G T Q S L N P H N D Y C Q H F V D T G H R P Q N F I R D V G L A D R F E E Y P K L R E L I R L K D E L I A K S N T P P M Y L Q A D I E A F D I R E L T P K F D V I L L E P P L E E Y Y R E T G I T A N E K C W T W D D I M K L E I D E I A A P R S F I F L W C G S G E G L D L G R V C L R K W G Y R R C E D I C W I K T N K N N P G K T K T L D P K A V F Q R T K E H C L M G I K G T V K R S T D G D F I H A N V D I D L I I T E E P E I G N I E K P V E I F H I I E H F C L G R R R L H L F G R D S T I R P G W L T V G P T L T N S N Y N A E T Y A S Y F S A P N S Y L T G C T E E I E R L R P K S P P P K S K S D R G G G A P R G G G R G G T S A G R G R E R N R S N F R G E R G G F R G G R G G A H R G G F P P R
50100150200250300350400450SequenceGHTBSN

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-Q9HCE5-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9HCE5-F1.cif  
DSSP Secondary Structures   Q9HCE5.dssp  





Diseases connected to this enzyme:

Publications:

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