Modomics - A Database of RNA Modifications

ID Card:

Full name: Elongator complex protein 2
Synonym: TOT2
GI: 1176045
Orf: G7725
COG: COG2319
UniProt: P42935
Structures: | 4XFV | 5M2N | 6QK7 |
Alpha Fold Predicted Structure: AF-P42935-F1
Complex: Elongator complex


PDB Structures:


4XFV

Structure Description:

Title: Crystal Structure of Elp2
Classification: TRANSLATION
Technique: X-Ray Diffraction
Resolution: 3.2
R value free: 0.241
R value observed: 0.199
R value work: 0.199

Abstract of the PDB Structure's related Publication:

Elongator is a highly conserved multiprotein complex composed of six subunits (Elp1-6). Elongator has been associated with various cellular activities and has attracted clinical attention because of its role in certain neurodegenerative diseases. Here, we present the crystal structure of the Elp2 subunit revealing two seven-bladed WD40 β propellers, and show by structure-guided mutational analyses that the WD40 fold integrity of Elp2 is necessary for its binding to Elp1 and Elp3 subunits in multiple species. The detailed biochemical experiments indicate that Elp2 binds microtubules through its conserved alkaline residues in vitro and in vivo. We find that both the mutually independent Elp2-mediated Elongator assembly and the cytoskeleton association are important for yeast viability. In addition, mutation of Elp2 greatly affects the histone H3 acetylation activity of Elongator in vivo. Our results indicate that Elp2 is a necessary component for functional Elongator and acts as a hub in the formation of various complexes.

Download RCSB-PDB Structures:

Pdb Files   4XFV.pdb   5M2N.pdb   6QK7.pdb  
Pdbx/mmCIF Files   4XFV.cif   5M2N.cif   6QK7.cif  


Protein sequence:

MVECITPEAIFIGANKQTQVSDIHKVKKIVAFGAGKTIALWDPIEPNNKGVYATLKGHEAEVTCVRFVPDSDFMVSASEDHHVKIWKFTDYSHLQCIQTIQHYSKTIVALSALPSLISVGCADGTISIWRQNIQNDEFGLAHEFTIKKGFFYPLCLSLSKVEEKKYLLAIGGTNVNVFIASFILSDSGIEKCRVVAELEGHEDWVKSLAFRHQETPGDYLLCSGSQDRYIRLWRIRINDLIDDSEEDSKKLTLLSNKQYKFQIDDELRVGINFEALIMGHDDWISSLQWHESRLQLLAATADTSLMVWEPDETSGIWVCSLRLGEMSSKGASTATGSSGGFWSCLWFTHERMDFFLTNGKTGSWRMWATKDNIICDQRLGISGATKDVTDIAWSPSGEYLLATSLDQTTRLFAPWIYDASGRKREIATWHEFSRPQIHGYDMICVETVTDTRFVSGGDEKILRSFDLPKGVAGMLQKFVGIQFEEKSEMPDSATVPVLGLSNKAGEDDANEDDEEEEGGNKETPDITDPLSLLECPPMEDQLQRHLLWPEVEKLYGHGFEITCLDISPDQKLIASACRSNNVQNAVIRIFSTENWLEIKPALPFHSLTITRLKFSKDGKFLLSVCRDRKWALWERNMEDNTFELRFKNEKPHTRIIWDADWAPLEFGNVFVTASRDKTVKVWRHQKEPADDYVLEASIKHTKAVTAISIHDSMIREKILISVGLENGEIYLYSYTLGKFELITQLNEDITPADKITRLRWSHLKRNGKLFLGVGSSDLSTRIYSLAYE

Comments:

One of the six protein cofactors required for the synthesis of 5-carboxymethyl group (cm5) on the wobble uridine-34 of a few tRNA. Acetate or acetyl-CoA is the donor of acetyl group, but the detailed mechanism of the reaction is still unknown. The cm5U derivative is the intermediate for further biochemical transformation of U34 derivative to either 5-methoxycarbonylmethyl uridine (mcm5U) catalysed by Trm9/Trm112 or 5-carbamoylmethyluridine (ncm5U) catalysed by a still unknown enzyme. Mutation in Elp (especially Elp3) influences telomeric gene silencing and DNA damage response. The multi-subunit complex El1-6 also interacts with elongating RNA polymerase II (RNAPII) is thought to facilitate transcription through histone acetylation.





Alpha Fold Predicted Structure:




Downloading... [122618/720339]


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Protein sequence:

M V E C I T P E A I F I G A N K Q T Q V S D I H K V K K I V A F G A G K T I A L W D P I E P N N K G V Y A T L K G H E A E V T C V R F V P D S D F M V S A S E D H H V K I W K F T D Y S H L Q C I Q T I Q H Y S K T I V A L S A L P S L I S V G C A D G T I S I W R Q N I Q N D E F G L A H E F T I K K G F F Y P L C L S L S K V E E K K Y L L A I G G T N V N V F I A S F I L S D S G I E K C R V V A E L E G H E D W V K S L A F R H Q E T P G D Y L L C S G S Q D R Y I R L W R I R I N D L I D D S E E D S K K L T L L S N K Q Y K F Q I D D E L R V G I N F E A L I M G H D D W I S S L Q W H E S R L Q L L A A T A D T S L M V W E P D E T S G I W V C S L R L G E M S S K G A S T A T G S S G G F W S C L W F T H E R M D F F L T N G K T G S W R M W A T K D N I I C D Q R L G I S G A T K D V T D I A W S P S G E Y L L A T S L D Q T T R L F A P W I Y D A S G R K R E I A T W H E F S R P Q I H G Y D M I C V E T V T D T R F V S G G D E K I L R S F D L P K G V A G M L Q K F V G I Q F E E K S E M P D S A T V P V L G L S N K A G E D D A N E D D E E E E G G N K E T P D I T D P L S L L E C P P M E D Q L Q R H L L W P E V E K L Y G H G F E I T C L D I S P D Q K L I A S A C R S N N V Q N A V I R I F S T E N W L E I K P A L P F H S L T I T R L K F S K D G K F L L S V C R D R K W A L W E R N M E D N T F E L R F K N E K P H T R I I W D A D W A P L E F G N V F V T A S R D K T V K V W R H Q K E P A D D Y V L E A S I K H T K A V T A I S I H D S M I R E K I L I S V G L E N G E I Y L Y S Y T L G K F E L I T Q L N E D I T P A D K I T R L R W S H L K R N G K L F L G V G S S D L S T R I Y S L A Y E
100200300400500600700SequenceGHTBSN

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-P42935-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P42935-F1.cif  
DSSP Secondary Structures   P42935.dssp  





Publications: