Aug 18, 2014 · Cys134 in SpoIIIJ is conserved among orthologues of the protein, as shown in the alignment of Fig. S3A. A cysteine residue is found at the homologous position of YqjG (Cys142), the other member of the YidC/Oxa1/Alb3 family found in B. subtilis, and also in the E. coli YidC protein. A single serine residue determines selectivity to Here we show that the presence of alanine at this position does not modify the activation pattern of monovalent metal sensors. In contrast, GolS or CueR mutant sensors with a substitution of cysteine for the serine residue respond to monovalent metal ions or Hg(II) with high sensitivities.
2.4 Cysteine gatekeeper alternative. In extreme cases where glycine and alanine residues are not tolerated at the gatekeeper position, our lab has developed an approach that utilizes a cysteine gatekeeper (Garske, Peters, Cortesi, Perez, & Shokat, 2011). This engineered kinase is termed an ES kinase and relies on inhibitors that target the cysteine gatekeeper through covalent chemistry. Essential Cysteine Residues in Bacillus subtilis Spore Sep 16, 2005 · To probe the function of the fourth cysteine, each conserved cysteine in the B. subtilis SP lyase was systematically altered to alanine by site-directed mutagenesis. UV-visible spectroscopy of wild-type and mutant SP lyases indicated that C141 does not participate in [4Fe-4S] formation and redox chemistry; however, in vivo SP lyase activity was abolished in all mutants, indicating an essential role Identification of the reactive cysteine residue (Cys227 Dec 25, 2001 · Structurally, carbonyl reductase belongs to the short-chain dehydrogenase/reductase family and contains five cysteine residues, none of which is conserved within the family. In order to identify the reactive residue and investigate its possible role in glutathione binding, alanine was substituted for each cysteine residue of human carbonyl
acids. The protein actually contains four cysteine residues. One residue is located in the hydrophobic domain at position 23, whereas three of these residues are present at positions 40, 44, and 47 adjacent to the hydrophobic domain. We investigated the functional signicance of the conserved residues using re-verse genetics. Sequence determinants directing conversion of cysteine translational modication, an -formylglycine residue that is essential for enzyme activity. Formylglycine is generated by oxidation of a conserved cysteine or, in some prokaryotic sulfatases, serine residue. In eukaryotes, this oxidation occurs in the endoplasmic reticulum during or shortly after import of the The conserved aromatic residue W122 is a determinant The conserved aromatic residue W122 is a determinant of potyviral coat protein stability, replication, and cell-to-cell to the codons for residue alanine (A), glutamic acid (E), or lysine cysteine (C), or E; serine at position 92
Jun 06, 2011 · disrupted mutations, substitution of the polar residue seryl for cystei-nyl restored normal function in one (C415S) but not the other (C124S). We assessed the relationship of prestin oligomerization to cysteine position using uorescence resonance energy transfer. With one exception, cysteine-alanine substitutions did not signicantly alterCatalytic role of a conserved cysteine residue in the Jan 01, 2010 · Substitution of the cysteine residue to alanine, valine, and serine resulted in an active luciferase enzyme with decreased bioluminescence. Although the rate of formation of the C4a-(hydro)peroxyflavin intermediate was not compromised in these variants, the rate of decay for the flavin intermediate was increased relative to wild-type .