2LM4

Solution NMR Structure of mitochondrial succinate dehydrogenase assembly factor 2 from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium Target YT682A


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution NMR structure of yeast succinate dehydrogenase flavinylation factor sdh5 reveals a putative sdh1 binding site.

Eletsky, A.Jeong, M.Y.Kim, H.Lee, H.W.Xiao, R.Pagliarini, D.J.Prestegard, J.H.Winge, D.R.Montelione, G.T.Szyperski, T.

(2012) Biochemistry 51: 8475-8477

  • DOI: https://doi.org/10.1021/bi301171u
  • Primary Citation of Related Structures:  
    2LM4

  • PubMed Abstract: 

    The yeast mitochondrial protein Sdh5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a subunit of the heterotetrameric enzyme succinate dehydrogenase. The NMR structure of Sdh5 represents the first eukaryotic structure of Pfam family PF03937 and reveals a conserved surface region, which likely represents a putative Sdh1-Sdh5 interaction interface. Point mutations in this region result in the loss of covalent flavinylation of Sdh1. Moreover, chemical shift perturbation measurements showed that Sdh5 does not bind FAD in vitro, indicating that it is not a simple cofactor transporter in vivo.


  • Organizational Affiliation

    Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Succinate dehydrogenase assembly factor 2, mitochondrial109Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: EMI5SDH5YOL071W
UniProt
Find proteins for Q08230 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q08230 
Go to UniProtKB:  Q08230
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ08230
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2012-01-04
    Type: Initial release
  • Version 1.1: 2012-12-05
    Changes: Database references
  • Version 1.2: 2013-01-30
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Data collection, Database references, Other