Modomics - A Database of RNA Modifications

ID Card:

Full name: H/ACA ribonucleoprotein complex subunit DKC1
Synonym: NOLA4
GI: 3913488
UniProt: O60832
Structures: | 7BGB | 7TRC | 7V9A |
Alpha Fold Predicted Structure: AF-O60832-F1


PDB Structures:


7BGB

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

Telomerase adds telomeric repeats at chromosome ends to compensate for the telomere loss that is caused by incomplete genome end replication 1 . In humans, telomerase is upregulated during embryogenesis and in cancers, and mutations that compromise the function of telomerase result in disease 2 . A previous structure of human telomerase at a resolution of 8 Å revealed a vertebrate-specific composition and architecture 3 , comprising a catalytic core that is flexibly tethered to an H and ACA (hereafter, H/ACA) box ribonucleoprotein (RNP) lobe by telomerase RNA. High-resolution structural information is necessary to develop treatments that can effectively modulate telomerase activity as a therapeutic approach against cancers and disease. Here we used cryo-electron microscopy to determine the structure of human telomerase holoenzyme bound to telomeric DNA at sub-4 Å resolution, which reveals crucial DNA- and RNA-binding interfaces in the active site of telomerase as well as the locations of mutations that alter telomerase activity. We identified a histone H2A-H2B dimer within the holoenzyme that was bound to an essential telomerase RNA motif, which suggests a role for histones in the folding and function of telomerase RNA. Furthermore, this structure of a eukaryotic H/ACA RNP reveals the molecular recognition of conserved RNA and protein motifs, as well as interactions that are crucial for understanding the molecular pathology of many mutations that cause disease. Our findings provide the structural details of the assembly and active site of human telomerase, which paves the way for the development of therapeutic agents that target this enzyme.

Download RCSB-PDB Structures:

Pdb Files   7BGB.pdb   7TRC.pdb   7V9A.pdb  
Pdbx/mmCIF Files   7BGB.cif   7TRC.cif   7V9A.cif  


Protein sequence:

MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYSESAKKEVVAEVVKAPQVVAEAAKTAKRKRESESESDETPPAAPQLIKKEKKKSKKDKKAKAGLESGAEPGDGDSDTTKKKKKKKKAKEVELVSE

Comments:





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

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

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-O60832-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-O60832-F1.cif  
DSSP Secondary Structures   O60832.dssp  





Diseases connected to this enzyme:

Description Reaction Disease Name
DKC1 encodes dykerin which can induce the pseudoridylation of rRNA. Defects in the pseudouridylation activity of dyskerin is related to the development of malignancy in patients with DC U:Y
Metachronous rectal adenocarcinomas with dyskeratosis congenita (DC)

Publications:

Title Authors Journal Details PubMed Id DOI