Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA (cytosine-5-)-methyltransferase NSUN6
GI: 1189131264
UniProt: Q8TEA1
Structures: | 5WWT | 5WWQ | 5WWR | 5WWS |
Alpha Fold Predicted Structure: AF-Q8TEA1-F1
Enzyme type: methyltransferase


PDB Structures:


5WWT

Structure Description:

Title: Crystal structure of human NSun6
Classification: TRANSFERASE
Technique: X-Ray Diffraction
Resolution: 2.81
R value free: 0.267
R value observed: 0.23
R value work: 0.229

Abstract of the PDB Structure's related Publication:

5-methylcytosine (m5C) modifications of RNA are ubiquitous in nature and play important roles in many biological processes such as protein translational regulation, RNA processing and stress response. Aberrant expressions of RNA:m5C methyltransferases are closely associated with various human diseases including cancers. However, no structural information for RNA-bound RNA:m5C methyltransferase was available until now, hindering elucidation of the catalytic mechanism behind RNA:m5C methylation. Here, we have solved the structures of NSun6, a human tRNA:m5C methyltransferase, in the apo form and in complex with a full-length tRNA substrate. These structures show a non-canonical conformation of the bound tRNA, rendering the base moiety of the target cytosine accessible to the enzyme for methylation. Further biochemical assays reveal the critical, but distinct, roles of two conserved cysteine residues for the RNA:m5C methylation. Collectively, for the first time, we have solved the complex structure of a RNA:m5C methyltransferase and addressed the catalytic mechanism of the RNA:m5C methyltransferase family, which may allow for structure-based drug design toward RNA:m5C methyltransferase-related diseases.

Download RCSB-PDB Structures:

Pdb Files   5WWQ.pdb   5WWR.pdb   5WWS.pdb   5WWT.pdb  
Pdbx/mmCIF Files   5WWQ.cif   5WWR.cif   5WWS.cif   5WWT.cif  


Protein sequence:

MSIFPKISLRPEVENYLKEGFMNKEIVTALGKQEAERKFETLLKHLSHPPSFTTVRVNTHLASVQHVKNLLLDELQKQFNGLSVPILQHPDLQDVLLIPVIGPRKNIKKQQCEAIVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKCKKGAKEFDGTKVFLGNGISELSRKEIFSGLPELKGMGIRMTEPVYLSPSFDSVLPRYLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKLDMVEDTEGEPPFLPESFDRILLDAPCSGMGQRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQLQRFDPSAVPLPDTDMDSLREARREDMLRLANKDSIGFFIAKFVKCKST

Comments:





Alpha Fold Predicted Structure:




Parsing response... [421862/421862]


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Protein sequence:

M S I F P K I S L R P E V E N Y L K E G F M N K E I V T A L G K Q E A E R K F E T L L K H L S H P P S F T T V R V N T H L A S V Q H V K N L L L D E L Q K Q F N G L S V P I L Q H P D L Q D V L L I P V I G P R K N I K K Q Q C E A I V G A Q C G N A V L R G A H V Y A P G I V S A S Q F M K A G D V I S V Y S D I K G K C K K G A K E F D G T K V F L G N G I S E L S R K E I F S G L P E L K G M G I R M T E P V Y L S P S F D S V L P R Y L F L Q N L P S A L V S H V L N P Q P G E K I L D L C A A P G G K T T H I A A L M H D Q G E V I A L D K I F N K V E K I K Q N A L L L G L N S I R A F C F D G T K A V K L D M V E D T E G E P P F L P E S F D R I L L D A P C S G M G Q R P N M A C T W S V K E V A S Y Q P L Q R K L F T A A V Q L L K P E G V L V Y S T C T I T L A E N E E Q V A W A L T K F P C L Q L Q P Q E P Q I G G E G M R G A G L S C E Q L K Q L Q R F D P S A V P L P D T D M D S L R E A R R E D M L R L A N K D S I G F F I A K F V K C K S T
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-Q8TEA1-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q8TEA1-F1.cif  
DSSP Secondary Structures   Q8TEA1.dssp  





Diseases connected to this enzyme:

Publications: