Modomics - A Database of RNA Modifications

ID Card:

Full name: NOP56 ribonucleoprotein
Synonym: SCA36
GI: 117949609
UniProt: O00567
Structures: | 7MQ8 | 7MQ9 | 7MQA |
Alpha Fold Predicted Structure: AF-O00567-F1


PDB Structures:


7MQ8

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

The human small subunit processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps. We report the high-resolution cryo–electron microscopy structures of maturing human small subunit (SSU) processomes at resolutions of 2.7 to 3.9 angstroms. These structures reveal the molecular mechanisms that enable crucial progressions during SSU processome maturation. RNA folding states within these particles are communicated to and coordinated with key enzymes that drive irreversible steps such as targeted exosome-mediated RNA degradation, protein-guided site-specific endonucleolytic RNA cleavage, and tightly controlled RNA unwinding. These conserved mechanisms highlight the SSU processome’s impressive structural plasticity, which endows this 4.5-megadalton nucleolar assembly with the distinctive ability to mature the small ribosomal subunit from within.

Download RCSB-PDB Structures:

Pdb Files  
Pdbx/mmCIF Files   7MQ8.cif   7MQ9.cif   7MQA.cif  


Protein sequence:

MVLLHVLFEHAVGYALLALKEVEEISLLQPQVEESVLNLGKFHSIVRLVAFCPFASSQVALENANAVSEGVVHEDLRLLLETHLPSKKKKVLLGVGDPKIGAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGHSYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPELVKIINDNATYCRLAQFIGNRRELNEDKLEKLEELTMDGAKAKAILDASRSSMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALIGEAVGARLIAHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGLIFHSTFIGRAAAKNKGRISRYLANKCSIASRIDCFSEVPTSVFGEKLREQVEERLSFYETGEIPRKNLDVMKEAMVQAEEAAAEITRKLEKQEKKRLKKEKKRLAALALASSENSSSTPEECEEMSEKPKKKKKQKPQEVPQENGMEDPSISFSKPKKKKSFSKEELMSSDLEETAGSTSIPKRKKSTPKEETVNDPEEAGHRSGSKKKRKFSKEEPVSSGPEEAVGKSSSKKKKKFHKASQED

Comments:

None





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

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

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-O00567-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-O00567-F1.cif  
DSSP Secondary Structures   O00567.dssp  





Diseases connected to this enzyme:

Description Reaction Disease Name
Inhibition of the production of properly modified leading to impaired proliferation and differentiation of specific embryonic cells. Downregulated expression of treacle resulted in decrease 2'-O-Me of 18S pre-rRNA N:Nm
Treacher Collins syndrome

Publications:

Title Authors Journal Details PubMed Id DOI