6H05

Cryo-electron microscopic structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate (2-oxoglutarate) dehydrogenase complex [residues 218-453]

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: Implications for the overall hKGDHc structure.

Nagy, B., Polak, M., Ozohanics, O., Zambo, Z., Szabo, E., Hubert, A., Jordan, F., Novacek, J., Adam-Vizi, V., Ambrus, A.

(2021) Biochim Biophys Acta Gen Subj 1865: 129889-129889

  • DOI: https://doi.org/10.1016/j.bbagen.2021.129889
  • Primary Citation of Related Structures:  
    6H05

  • PubMed Abstract: 

    The human mitochondrial alpha-ketoglutarate dehydrogenase complex (hKGDHc) converts KG to succinyl-CoA and NADH. Malfunction of and reactive oxygen species generation by the hKGDHc as well as its E1-E2 subcomplex are implicated in neurodegenerative disorders, ischemia-reperfusion injury, E3-deficiency and cancers.

    • Organizational Affiliation: 

    Department of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial426Homo sapiensMutation(s): 0 
Gene Names: DLST, DLTS
EC: 2.3.1.61
UniProt & NIH Common Fund Data Resources
Find proteins for P36957 (Homo sapiens)
Explore P36957 
Go to UniProtKB:  P36957
PHAROS:  P36957
GTEx:  ENSG00000119689 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP36957
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX
RECONSTRUCTIONcryoSPARC

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Hungarian Academy of SciencesHungaryMTA grant 02001 (to Vera Adam-Vizi)
Hungarian Academy of SciencesHungaryOTKA grant 112230 (to Vera Adam-Vizi)
Hungarian Academy of SciencesHungaryNAP grant KTIA_13_NAP-A-III/6 (to Vera Adam-Vizi)
Hungarian Academy of SciencesHungaryNAP 2 grant 2017-1.2.1-NKP- 2017-00002 (to Vera Adam-Vizi)
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesNIH-GM-050380 (to Frank Jordan)
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesNIH R15-GM116077 (to Frank Jordan)

Revision History  (Full details and data files)

  • Version 1.0: 2020-01-22
    Type: Initial release
  • Version 1.1: 2021-04-07
    Changes: Database references