1F6Y

MAD CRYSTAL STRUCTURE ANALYSIS OF METHYLTETRAHYDROFOLATE: CORRINOID/IRON-SULFUR PROTEIN METHYLTRANSFERASE (METR)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.

Doukov, T.Seravalli, J.Stezowski, J.J.Ragsdale, S.W.

(2000) Structure 8: 817-830

  • DOI: https://doi.org/10.1016/s0969-2126(00)00172-6
  • Primary Citation of Related Structures:  
    1F6Y

  • PubMed Abstract: 

    Methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr), catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide center in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin. We report the first structure of a protein in this family.


  • Organizational Affiliation

    Department of Chemistry, University of Nebraska-Lincoln, 68503, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
5-METHYLTETRAHYDROFOLATE CORRINOID/IRON SULFUR PROTEIN METHYLTRANSFERASE
A, B
262Moorella thermoacetica ATCC 39073Mutation(s): 0 
UniProt
Find proteins for Q46389 (Moorella thermoacetica)
Explore Q46389 
Go to UniProtKB:  Q46389
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ46389
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.206 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 65α = 90
b = 89.412β = 90
c = 115.385γ = 90
Software Package:
Software NamePurpose
SHELXSphasing
SHELXL-97refinement
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-08-31
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description
  • Version 1.4: 2018-01-31
    Changes: Database references
  • Version 1.5: 2024-02-07
    Changes: Data collection, Database references