1YUB

SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 17 
  • Conformers Submitted: 
  • Selection Criteria: LOWEST ENERGY AND LEAST RESTRAINT VIOLATION 

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This is version 1.3 of the entry. See complete history


Literature

Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.

Yu, L.Petros, A.M.Schnuchel, A.Zhong, P.Severin, J.M.Walter, K.Holzman, T.F.Fesik, S.W.

(1997) Nat Struct Biol 4: 483-489

  • DOI: https://doi.org/10.1038/nsb0697-483
  • Primary Citation of Related Structures:  
    1YUB

  • PubMed Abstract: 

    The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices.


  • Organizational Affiliation

    Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RRNA METHYLTRANSFERASE245Streptococcus pneumoniaeMutation(s): 0 
Gene Names: ERM
EC: 2.1.1.48
UniProt
Find proteins for P21236 (Streptococcus pneumoniae)
Explore P21236 
Go to UniProtKB:  P21236
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP21236
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 17 
  • Conformers Submitted: 
  • Selection Criteria: LOWEST ENERGY AND LEAST RESTRAINT VIOLATION 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-03-04
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations, Other