Database accession: MF7000866
Name: Erv2p
PDB ID: 1jr8
Experimental method: X-ray (1.50 Å)
Assembly: Homodimer
Source organism: Saccharomyces cerevisiae
Primary publication of the structure:
Gross E, Sevier CS, Vala A, Kaiser CA, Fass D
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
(2002) Nat. Struct. Biol. 9: 61-7
PMID: 11740506
Abstract:
Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can swing into the vicinity of the first cysteine pair in the opposite subunit of the dimer and may shuttle electrons between substrate protein dithiols and the FAD-proximal disulfide.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
flavin adenine dinucleotide binding flavin adenine dinucleotide binding
flavin-dependent sulfhydryl oxidase activity flavin-dependent sulfhydryl oxidase activity
thiol oxidase activity thiol oxidase activity
Biological process:
regulation of protein folding in endoplasmic reticulum regulation of protein folding in endoplasmic reticulum
Cellular component:
endoplasmic reticulum membrane endoplasmic reticulum membrane
fungal-type vacuole fungal-type vacuole
fungal-type vacuole membrane fungal-type vacuole 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: FAD-linked sulfhydryl oxidase ERV2
Source organism: Saccharomyces cerevisiae
Length: 196 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG
UniProtKB AC: Q12284 (positions: 74-178)
Coverage: 53%
Name: FAD-linked sulfhydryl oxidase ERV2
Source organism: Saccharomyces cerevisiae
Length: 196 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG
UniProtKB AC: Q12284 (positions: 75-179)
Coverage: 53%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: ERV/ALR sulfhydryl oxidase domain
Evidence level: Insufficient evidence (candidate)
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface.
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)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
