Database accession: MF7000740
Name: N-terminal cytoplasmic tethering domain of mitoNEET
PDB ID: 3ew0
Experimental method: X-ray (1.40 Å)
Assembly: Homodimer
Source organism: Homo sapiens
Primary publication of the structure:
Conlan AR, Paddock ML, Axelrod HL, Cohen AE, Abresch EC, Wiley S, Roy M, Nechushtai R, Jennings PA
The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain.
(2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65: 654-9
PMID: 19574633
Abstract:
A primary role for mitochondrial dysfunction is indicated in the pathogenesis of insulin resistance. A widely used drug for the treatment of type 2 diabetes is pioglitazone, a member of the thiazolidinedione class of molecules. MitoNEET, a 2Fe-2S outer mitochondrial membrane protein, binds pioglitazone [Colca et al. (2004), Am. J. Physiol. Endocrinol. Metab. 286, E252-E260]. The soluble domain of the human mitoNEET protein has been expressed C-terminal to the superfolder green fluorescent protein and the mitoNEET protein has been isolated. Comparison of the crystal structure of mitoNEET isolated from cleavage of the fusion protein (1.4 A resolution, R factor = 20.2%) with other solved structures shows that the CDGSH domains are superimposable, indicating proper assembly of mitoNEET. Furthermore, there is considerable flexibility in the position of the cytoplasmic tethering arms, resulting in two different conformations in the crystal structure. This flexibility affords multiple orientations on the outer mitochondrial membrane.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
2 iron, 2 sulfur cluster binding 2 iron, 2 sulfur cluster binding
identical protein binding identical protein binding
L-cysteine transaminase activity L-cysteine transaminase activity
metal ion binding metal ion binding
protein homodimerization activity protein homodimerization activity
pyridoxal phosphate binding pyridoxal phosphate binding
Biological process:
protein maturation by [2Fe-2S] cluster transfer protein maturation by [2Fe-2S] cluster transfer
regulation of autophagy regulation of autophagy
regulation of cellular respiration regulation of cellular respiration
Cellular component:
mitochondrial outer membrane mitochondrial outer membrane
mitochondrion mitochondrion
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: CDGSH iron-sulfur domain-containing protein 1
Source organism: Homo sapiens
Length: 108 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET
UniProtKB AC: Q9NZ45 (positions: 33-107)
Coverage: 69%
Name: CDGSH iron-sulfur domain-containing protein 1
Source organism: Homo sapiens
Length: 108 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET
UniProtKB AC: Q9NZ45 (positions: 33-104)
Coverage: 66%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Iron-binding zinc finger CDGSH type
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
Size exclusion chromatography measurements suggest that mitoNEET33–108 protein exists as a dimer in solution (PMID:17905743). The monomers associate along their full length to form an intertwined structure with an extensive interface (PMID:17766439).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
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