Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA wyosine derivatives biosynthesis protein Taw1
Synonym: Tyw1
GI: 74571635
Orf: PH1705
COG: COG0731
UniProt: O59412
Structures: | 2YX0 |
Alpha Fold Predicted Structure: AF-O59412-F1
Enzyme type: oxidoreductase


PDB Structures:


2YX0

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

Wye bases are tricyclic bases that are found in archaeal and eukaryotic tRNAs. The most modified wye base, wybutosine, which appears at position 37 (the 3'-adjacent position to the anticodon), is known to be important for translational reading-frame maintenance. Saccharomyces cerevisiae TYW1 catalyzes the tri-ring-formation step in wye-base biosynthesis, with the substrate tRNA bearing N(1)-methylated G37. Here, the crystal structure of the archaeal TYW1 homologue from Pyrococcus horikoshii is reported at 2.2 A resolution. The amino-acid sequence of P. horikoshii TYW1 suggested that it is a radical-AdoMet enzyme and the tertiary structure of P. horikoshii TYW1 indeed shares the modified TIM-barrel structure found in other radical-AdoMet enzymes. Radical-AdoMet enzymes generally contain one or two iron-sulfur (FeS) clusters. The tertiary structure of P. horikoshii TYW1 revealed two FeS cluster sites, each containing three cysteine residues. One FeS cluster site was expected from the amino-acid sequence and the other involves cysteine residues that are dispersed throughout the sequence. The existence of two FeS clusters was confirmed from the anomalous Fourier electron-density map. By superposing the P. horikoshii TYW1 tertiary structure on those of other radical-AdoMet enzymes, the AdoMet molecule, which is necessary for the reactions of radical-AdoMet enzymes, was modelled in P. horikoshii TYW1. Surface plots of conservation rates and electrostatic potentials revealed the highly conserved and positively charged active-site hollow. On the basis of the surface properties, a docking model of P. horikoshii TYW1, the tRNA, the FeS clusters and the AdoMet molecule was constructed, with the nucleoside at position 37 of tRNA flipped out from the canonical tRNA structure.

Download RCSB-PDB Structures:

Pdb Files   2YX0.pdb  
Pdbx/mmCIF Files   2YX0.cif  


Protein sequence:

MMEMITIKPGKITVQANPNMPKEVAELFRKQHYEIVGRHSGVKLCHWLKKSLTEGRFCYKQKFYGIHSHRCLQMTPVLAWCTHNCIFCWRPMENFLGTELPQPWDDPAFIVEESIKAQRKLLIGYKGNPKVDKKKFEEAWNPTHAAISLSGEPMLYPYMGDLVEEFHKRGFTTFIVTNGTIPERLEEMIKEDKLPTQLYVSITAPDIETYNSVNIPMIPDGWERILRFLELMRDLPTRTVVRLTLVKGENMHSPEKYAKLILKARPMFVEAKAYMFVGYSRNRLTINNMPSHQDIREFAEALVKHLPGYHIEDEYEPSRVVLIMRDDVDPQGTGVEGRFIKH

Comments:

Homologue of yeast Tyw1. Does not have the N-terminal FMN binding/flavodoxin domain found in Tyw1. Predicted to participate in the m1G:imG-14 reaction.





Alpha Fold Predicted Structure:






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Protein sequence:

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

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-O59412-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-O59412-F1.cif  
DSSP Secondary Structures   O59412.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea. de Crecy-Lagard V, Brochier-Armanet C, Urbonavicius J, Fernandez B, Phillips G, Lyons B, Noma A, Alvarez S, Droogmans L, Armengaud J, Grosjean H Mol Biol Evol [details] 20382657 -
Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis. Goto-Ito S, Ishii R, Ito T, Shibata R, Fusatomi E, Sekine SI, Bessho Y, Yokoyama S Acta Crystallogr D Biol Crystallogr [details] 17881823 -