Database accession: MF7000870
Name: Human ALR, selenium substituted
PDB ID: 3u5s
Experimental method: X-ray (1.50 Å)
Assembly: Homodimer
Source organism: Homo sapiens
Primary publication of the structure:
Schaefer SA, Dong M, Rubenstein RP, Wilkie WA, Bahnson BJ, Thorpe C, Rozovsky S
(77)Se enrichment of proteins expands the biological NMR toolbox.
(2013) J. Mol. Biol. 425: 222-31
PMID: 23159557
Abstract:
Sulfur, a key contributor to biological reactivity, is not amendable to investigations by biological NMR spectroscopy. To utilize selenium as a surrogate, we have developed a generally applicable (77)Se isotopic enrichment method for heterologous proteins expressed in Escherichia coli. We demonstrate (77)Se NMR spectroscopy of multiple selenocysteine and selenomethionine residues in the sulfhydryl oxidase augmenter of liver regeneration (ALR). The resonances of the active-site residues were assigned by comparing the NMR spectra of ALR bound to oxidized and reduced flavin adenine dinucleotide. An additional resonance appears only in the presence of the reducing agent and disappears readily upon exposure to air and subsequent reoxidation of the flavin. Hence, (77)Se NMR spectroscopy can be used to report the local electronic environment of reactive and structural sulfur sites, as well as changes taking place in those locations during catalysis.
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
growth factor activity growth factor activity
protein-disulfide reductase activity protein-disulfide reductase activity
Biological process:
cellular response to actinomycin D cellular response to actinomycin D
cellular response to lipopolysaccharide cellular response to lipopolysaccharide
cellular response to toxic substance cellular response to toxic substance
cellular response to tumor necrosis factor cellular response to tumor necrosis factor
liver development liver development
liver regeneration liver regeneration
negative regulation of apoptotic process negative regulation of apoptotic process
negative regulation of natural killer cell mediated cytotoxicity negative regulation of natural killer cell mediated cytotoxicity
positive regulation of DNA biosynthetic process positive regulation of DNA biosynthetic process
Cellular component:
cytosol cytosol
extracellular space extracellular space
mitochondrial intermembrane space mitochondrial intermembrane space
mitochondrion mitochondrion
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
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 ALR
Source organism: Homo sapiens
Length: 205 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD
UniProtKB AC: P55789 (positions: 82-205)
Coverage: 60%
Name: FAD-linked sulfhydryl oxidase ALR
Source organism: Homo sapiens
Length: 205 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD
UniProtKB AC: P55789 (positions: 82-205)
Coverage: 60%
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 A-2:
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)
