Modomics - A Database of RNA Modifications

ID Card:

Full name: rRNA (uridine-2'-O-)-methyltransferase
Synonym: avilamycin resistance 23S rRNA methyltransferase
GI: 60593969
Orf: aviRb
COG: COG0566
UniProt: Q9F5K6
Structures: | 1X7O | 1X7P |
Alpha Fold Predicted Structure: AF-Q9F5K6-F1
Enzyme type: methyltransferase
Position of modification - modification: l:2479(2479) - Um


PDB Structures:


1X7O

Structure Description:

Title: Crystal structure of the SpoU Methyltransferase AviRb from Streptomyces viridochromogenes
Classification: TRANSFERASE
Technique: X-Ray Diffraction
Resolution: 2.37
R value free: 0.249
R value observed: 0.208
R value work: 0.206

Abstract of the PDB Structure's related Publication:

The emergence of antibiotic-resistant bacterial strains is a widespread problem in medical practice and drug design, and each case requires the elucidation of the underlying mechanism. AviRb from Streptomyces viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal RNA in Gram-positive bacteria and thus mediates resistance to the oligosaccharide (orthosomycin) antibiotic avilamycin. The structure of AviRb with and without bound cofactor S-adenosyl-L-methionine (AdoMet) was determined, showing that it is a homodimer belonging to the SpoU family within the SPOUT class of methyltransferases. The relationships within this class were analyzed in detail and, in addition, a novel fourth SpoU sequence fingerprint is proposed. Each subunit of AviRb consists of two domains. The N-terminal domain, being related to the ribosomal proteins L30 and L7Ae, is likely to bind RNA. The C-terminal domain is related to all SPOUT methyltransferases, and is responsible for AdoMet-binding, catalysis and dimerization. The cofactor binds at the characteristic knot of the polypeptide in an unusually bent conformation. The transferred methyl group points to a broad cleft formed with the L30-type domain of the other subunit. Measurements of mutant activity revealed four important residues responsible for catalysis and allowed the modeling of a complex between AviRb and the RNA target. The model includes a specificity pocket for uracil but does not contain a base for deprotonating the 2'-O atom of U2479 on methylation.

Download RCSB-PDB Structures:

Pdb Files   1X7O.pdb   1X7P.pdb  
Pdbx/mmCIF Files   1X7O.cif   1X7P.cif  


Protein sequence:

MARSRGERTPAARRITSRNARFQQWQALLGNRNKRTRAGEFLVMGVRPISLAVEHGWPVRTLLYDGQRELSKWARELLRTVRTEQIAMAPDLLMELGEKNEAPPEVVAVVEMPADDLDRIPVREDFLGVLFDRPTSPGNIGSIIRSADALGAHGLIVAGHAADVYDPKSVRSSTGSLFSLPAVRVPSPGEVMDWVEARRAAGTPIVLVGTDEHGDCDVFDFDFTQPTLLLIGNETAGLSNAWRTLCDYTVSIPMAGSASSLNAANAATAILYEAVRQRISGRTATTP

Comments:

Methylation site was determined for E. coli rRNA.





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M A R S R G E R T P A A R R I T S R N A R F Q Q W Q A L L G N R N K R T R A G E F L V M G V R P I S L A V E H G W P V R T L L Y D G Q R E L S K W A R E L L R T V R T E Q I A M A P D L L M E L G E K N E A P P E V V A V V E M P A D D L D R I P V R E D F L G V L F D R P T S P G N I G S I I R S A D A L G A H G L I V A G H A A D V Y D P K S V R S S T G S L F S L P A V R V P S P G E V M D W V E A R R A A G T P I V L V G T D E H G D C D V F D F D F T Q P T L L L I G N E T A G L S N A W R T L C D Y T V S I P M A G S A S S L N A A N A A T A I L Y E A V R Q R I S G R T A T T P
50100150200250SequenceGHTBSN

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-Q9F5K6-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9F5K6-F1.cif  
DSSP Secondary Structures   Q9F5K6.dssp  





Publications: