1BE1

GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 15 
  • Conformers Submitted: 
  • Selection Criteria: MINIMIZED AVERAGE 

wwPDB Validation   3D Report Full Report

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This is version 1.3 of the entry. See complete history


Literature

How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum

Tollinger, M.Konrat, R.Hilbert, B.H.Marsh, E.N.Krautler, B.

(1998) Structure 6: 1021-1033

  • DOI: https://doi.org/10.1016/s0969-2126(98)00103-8
  • Primary Citation of Related Structures:  
    1BE1

  • PubMed Abstract: 

    Glutamate mutase is an adenosylcobamide (coenzyme B12) dependent enzyme that catalyzes the reversible rearrangement of (2S)-glutamate to (2S,3S)-3-methylaspartate. The enzyme from Clostridium tetanomorphum comprises two subunits (of 53.7 and 14.8 kDa) and in its active form appears to be an alpha 2 beta 2 tetramer. The smaller subunit, termed MutS, has been characterized as the B12-binding component. Knowledge on the structure of a B12-binding apoenzyme does not exist.


  • Organizational Affiliation

    Institute of Organic Chemistry, University of Innsbruck, Austria.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLUTAMATE MUTASE137Clostridium tetanomorphumMutation(s): 0 
Gene Names: MUTS
EC: 5.4.99.1
UniProt
Find proteins for Q05488 (Clostridium tetanomorphum)
Explore Q05488 
Go to UniProtKB:  Q05488
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ05488
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 15 
  • Conformers Submitted: 
  • Selection Criteria: MINIMIZED AVERAGE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-08-26
    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: 2022-02-16
    Changes: Data collection, Database references, Derived calculations, Other