Modomics - A Database of RNA Modifications

ID Card:

Full name: Alpha-ketoglutarate-dependent dioxygenase FTO
Synonym: KIAA1752
GI: 122937263
UniProt: Q9C0B1
Structures: | 3LFM | 4CXW | 4CXX | 4CXY | 4IDZ | 4IE0 | 4IE4 | 4IE5 | 4IE6 | 4IE7 | 4QHO | 4QKN | 4ZS2 | 4ZS3 | 5DAB | 5F8P | 5ZMD | 6AEJ | 6AK4 | 6AKW | 7CKK | 7E8Z | 7WCV |
Alpha Fold Predicted Structure: AF-Q9C0B1-F1
Enzyme type: demethylase
Position of modification - modification: m:many - A
m:many - f6A
m:many - hm6A


PDB Structures:


3LFM

Structure Description:

Title: Crystal structure of the fat mass and obesity associated (FTO) protein reveals basis for its substrate specificity
Classification: OXIDOREDUCTASE
Technique: X-Ray Diffraction
Resolution: 2.5
R value free: 0.285
R value observed:
R value work: 0.239

Abstract of the PDB Structure's related Publication:

Recent studies have unequivocally associated the fat mass and obesity-associated (FTO) gene with the risk of obesity. In vitro FTO protein is an AlkB-like DNA/RNA demethylase with a strong preference for 3-methylthymidine (3-meT) in single-stranded DNA or 3-methyluracil (3-meU) in single-stranded RNA. Here we report the crystal structure of FTO in complex with the mononucleotide 3-meT. FTO comprises an amino-terminal AlkB-like domain and a carboxy-terminal domain with a novel fold. Biochemical assays show that these two domains interact with each other, which is required for FTO catalytic activity. In contrast with the structures of other AlkB members, FTO possesses an extra loop covering one side of the conserved jelly-roll motif. Structural comparison shows that this loop selectively competes with the unmethylated strand of the DNA duplex for binding to FTO, suggesting that it has an important role in FTO selection against double-stranded nucleic acids. The ability of FTO to distinguish 3-meT or 3-meU from other nucleotides is conferred by its hydrogen-bonding interaction with the two carbonyl oxygen atoms in 3-meT or 3-meU. Taken together, these results provide a structural basis for understanding FTO substrate-specificity, and serve as a foundation for the rational design of FTO inhibitors.

Download RCSB-PDB Structures:

Pdb Files   3LFM.pdb   4CXW.pdb   4CXX.pdb   4CXY.pdb   4IDZ.pdb   4IE0.pdb   4IE4.pdb   4IE5.pdb   4IE6.pdb   4IE7.pdb   4QHO.pdb   4QKN.pdb   4ZS2.pdb   4ZS3.pdb   5DAB.pdb   5F8P.pdb   5ZMD.pdb   6AEJ.pdb   6AK4.pdb   6AKW.pdb   7CKK.pdb   7E8Z.pdb   7WCV.pdb  
Pdbx/mmCIF Files   3LFM.cif   4CXW.cif   4CXX.cif   4CXY.cif   4IDZ.cif   4IE0.cif   4IE4.cif   4IE5.cif   4IE6.cif   4IE7.cif   4QHO.cif   4QKN.cif   4ZS2.cif   4ZS3.cif   5DAB.cif   5F8P.cif   5ZMD.cif   6AEJ.cif   6AK4.cif   6AKW.cif   7CKK.cif   7E8Z.cif   7WCV.cif  


Protein sequence:

MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCDDVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLPVEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP

Comments:

The human fat mass and obesity-associated protein FTO catalyses the removal of m6A in vitro and in vivo. It is a member of the non-haem FeII/a-ketoglutarate (a-KG)-dependent AlkB family demethylases that mainly catalyse oxidative demethylation of N-alkylated nucleic acid bases. FTO oxidizes m6A to hm6A and f6A in RNA in a step-wise manner. FTO was identified in several genome-wide-association studies to be associated with obesity and type II diabetes.





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M K R T P T A E E R E R E A K K L R L L E E L E D T W L P Y L T P K D D E F Y Q Q W Q L K Y P K L I L R E A S S V S E E L H K E V Q E A F L T L H K H G C L F R D L V R I Q G K D L L T P V S R I L I G N P G C T Y K Y L N T R L F T V P W P V K G S N I K H T E A E I A A A C E T F L K L N D Y L Q I E T I Q A L E E L A A K E K A N E D A V P L C M S A D F P R V G M G S S Y N G Q D E V D I K S R A A Y N V T L L N F M D P Q K M P Y L K E E P Y F G M G K M A V S W H H D E N L V D R S A V A V Y S Y S C E G P E E E S E D D S H L E G R D P D I W H V G F K I S W D I E T P G L A I P L H Q G D C Y F M L D D L N A T H Q H C V L A G S Q P R F S S T H R V A E C S T G T L D Y I L Q R C Q L A L Q N V C D D V D N D D V S L K S F E P A V L K Q G E E I H N E V E F E W L R Q F W F Q G N R Y R K C T D W W C Q P M A Q L E A L W K K M E G V T N A V L H E V K R E G L P V E Q R N E I L T A I L A S L T A R Q N L R R E W H A R C Q S R I A R T L P A D Q K P E C R P Y W E K D D A S M P L P F D L T D I V S E L R G Q L L E A K P
50100150200250300350400450500SequenceGHITBSN

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-Q9C0B1-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9C0B1-F1.cif  
DSSP Secondary Structures   Q9C0B1.dssp  





Diseases connected to this enzyme:

Publications:

Links:

_PubMed_