3U5S

Selenium Substituted Human Augmenter of Liver Regeneration

Summary for 3U5S

• Entry DOI: 10.2210/pdb3u5s/pdb
• Descriptor: FAD-linked sulfhydryl oxidase ALR, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: flavin, liver, oxidoreductase, selenium nmr, selenocysteine, selenoproteins, augmenter of liver regeneration
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Mitochondrion intermembrane space. Isoform 2: Cytoplasm: P55789
• Total number of polymer chains: 1
• Total formula weight: 16239.58

Authors

Dong, M.,Bahnson, B.J. (deposition date: 2011-10-11, release date: 2012-10-17, Last modification date: 2024-11-20)

Primary citation

Schaefer, S.A.,Dong, M.,Rubenstein, R.P.,Wilkie, W.A.,Bahnson, B.J.,Thorpe, C.,Rozovsky, S.
(77)Se enrichment of proteins expands the biological NMR toolbox.
J.Mol.Biol., 425:222-231, 2013

PubMed 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.

PubMed: 23159557
DOI: 10.1016/j.jmb.2012.11.011

Experimental method

X-RAY DIFFRACTION (1.5 Å)