Modomics - A Database of RNA Modifications

ID Card:

Full name: N6-adenosine-methyltransferase 70 kDa subunit
Synonym: MTA70
GI: 21361827
COG: COG4725
UniProt: Q86U44
Structures: | 5IL0 | 5IL1 | 5IL2 | 5K7M | 5K7U | 5K7W | 5L6D | 5L6E | 5TEY | 5YZ9 | 6TTP | 6TTT | 6TTV | 6TTW | 6TTX | 6TU1 | 6Y4G | 7ACD | 7O2I | 7O2X |
Alpha Fold Predicted Structure: AF-Q86U44-F1
Enzyme type: methyltransferase
Position of modification - modification: m:many - m6A


PDB Structures:


5IL0

Structure Description:

Title: Crystal structure of Sulfolobus solfataricus Nop5 (1-262) and fibrillarin complex
Classification: TRANSFERASE
Technique: X-Ray Diffraction
Resolution: 2.6
R value free: 0.285
R value observed: 0.235
R value work: 0.232

Abstract of the PDB Structure's related Publication:

Box C/D guide RNAs are abundant noncoding RNAs that primarily function to direct the 2'-O-methylation of specific nucleotides by base-pairing with substrate RNAs. In archaea, a bipartite C/D RNA assembles with L7Ae, Nop5, and the methyltransferase fibrillarin into a modification enzyme with unique substrate specificity. Here, we determined the crystal structure of an archaeal C/D RNA-protein complex (RNP) composed of all 3 core proteins and an engineered half-guide RNA at 4 A resolution, as well as 2 protein substructures at higher resolution. The RNP structure reveals that the C-terminal domains of Nop5 in the dimeric complex provide symmetric anchoring sites for 2 L7Ae-associated kink-turn motifs of the C/D RNA. A prominent protrusion in Nop5 seems to be important for guide RNA organization and function and for discriminating the structurally related U4 snRNA. Multiple conformations of the N-terminal domain of Nop5 and its associated fibrillarin in different structures indicate the inherent flexibility of the catalytic module, suggesting that a swinging motion of the catalytic module is part of the enzyme mechanism. We also built a model of a native C/D RNP with substrate and fibrillarin in an active conformation. Our results provide insight into the overall organization and mechanism of action of C/D RNA-guided RNA methyltransferases.

Download RCSB-PDB Structures:

Pdb Files   3ID6.pdb   5IL0.pdb   5IL1.pdb   5IL2.pdb   5K7M.pdb   5K7U.pdb   5K7W.pdb   5L6D.pdb   5L6E.pdb   5TEY.pdb   5YZ9.pdb   6TTP.pdb   6TTT.pdb   6TTV.pdb   6TTW.pdb   6TTX.pdb   6Y4G.pdb   7ACD.pdb   7O2I.pdb   7O2X.pdb  
Pdbx/mmCIF Files   3ID6.cif   5IL0.cif   5IL1.cif   5IL2.cif   5K7M.cif   5K7U.cif   5K7W.cif   5L6D.cif   5L6E.cif   5TEY.cif   5YZ9.cif   6TTP.cif   6TTT.cif   6TTV.cif   6TTW.cif   6TTX.cif   6Y4G.cif   7ACD.cif   7O2I.cif   7O2X.cif  


Protein sequence:

MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGGPKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLLQKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRAEQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSKKVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVGGDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL

Comments:

Forms a stable heterodimer with METTL14. The complex catalyses the AdoMet dependent N6-methylation of internal adenosine in mammalian mRNA. METTL3 displays a regulatory role on several cellular functions. METTL3 is critical for viability of mammalian cells. Notice, the methyl group of m6A in mRNA can be removed by the obesity-associated protein FTO (demethylase enzyme.)





Alpha Fold Predicted Structure:




Downloading... [110330/520033]


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Protein sequence:

M S D T W S S I Q A H K K Q L D S L R E R L Q R R R K Q D S G H L D L R N P E A A L S P T F R S D S P V P T A P T S G G P K P S T A S A V P E L A T D P E L E K K L L H H L S D L A L T L P T D A V S I C L A I S T P D A P A T Q D G V E S L L Q K F A A Q E L I E V K R G L L Q D D A H P T L V T Y A D H S K L S A M M G A V A E K K G P G E V A G T V T G Q K R R A E Q D S T T V A A F A S S L V S G L N S S A S E P A K E P A K K S R K H A A S D V D L E I E S L L N Q Q S T K E Q Q S K K V S Q E I L E L L N T T T A K E Q S I V E K F R S R G R A Q V Q E F C D Y G T K E E C M K A S D A D R P C R K L H F R R I I N K H T D E S L G D C S F L N T C F H M D T C K Y V H Y E I D A C M D S E A P G S K D H T P S Q E L A L T Q S V G G D S S A D R L F P P Q W I C C D I R Y L D V S I L G K F A V V M A D P P W D I H M E L P Y G T L T D D E M R R L N I P V L Q D D G F L F L W V T G R A M E L G R E C L N L W G Y E R V D E I I W V K T N Q L Q R I I R T G R T G H W L N H G K E H C L V G V K G N P Q G F N Q G L D C D V I V A E V R S T S H K P D E I Y G M I E R L S P G T R K I E L F G R P H N V Q P N W I T L G N Q L D G I H L L D P D V V A R F K Q R Y P D G I I S K P K N L
50100150200250300350400450500550SequenceGHTBSN

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-Q86U44-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q86U44-F1.cif  
DSSP Secondary Structures   Q86U44.dssp  





Diseases connected to this enzyme:

Publications:

Links:

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