2K32

Truncated AcrA from Campylobacter jejuni for glycosylation studies


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation.

Slynko, V.Schubert, M.Numao, S.Kowarik, M.Aebi, M.Allain, F.H.

(2009) J Am Chem Soc 131: 1274-1281

  • DOI: https://doi.org/10.1021/ja808682v
  • Primary Citation of Related Structures:  
    2K32, 2K33

  • PubMed Abstract: 

    Although there is great interest in three-dimensional structures of glycoproteins and complex oligosaccharides, their structural determination have been hampered by inhomogeneous and incomplete glycosylation, poor expression, low tendency to crystallize, and severe chemical shift overlap. Using segmental labeling of the glycan and the protein component by in vitro glycosylation, we developed a novel method of NMR structural determination that overcomes some of these problems. Highly homogeneously glycosylated proteins in milligram amounts can be obtained. This allowed the determination of the structure of an N-linked glycoprotein from Campylobacter jejuni. The glycosylation acceptor site was found to be in a flexible loop. The presented methodology extends the observable NOE distance limit of oligosaccharides significantly over 4 A, resulting in a high number of distance restraints per glycosidic linkage. A well-defined glycan structure was obtained.


  • Organizational Affiliation

    Institute of Molecular Biology and Biophysics, ETH Zurich, CH-8093 Zurich, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
A116Campylobacter jejuniMutation(s): 2 
Gene Names: cmeA
UniProt
Find proteins for Q8RTE5 (Campylobacter jejuni)
Explore Q8RTE5 
Go to UniProtKB:  Q8RTE5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8RTE5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-02-03
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-10-20
    Changes: Data collection, Database references, Derived calculations
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references