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- Fellner, Matthias; Rankin, Joel A.; Desguin, Benoît; Hu, Jian; Hausinger, Robert P.
- Biochemistry 2018 v.57 no.38 pp. 5513-5523
- Lactobacillus plantarum; Thermoanaerobacterium thermosaccharolyticum; active sites; adenosine triphosphate; apoproteins; biosynthesis; chemical bonding; coenzyme A; crystal structure; cysteine; lactic acid; models; sulfur; transferases
- ... LarE from Lactobacillus plantarum is an ATP-dependent sulfur transferase that sacrifices its Cys176 sulfur atom to form a dehydroalanine (Dha) side chain during biosynthesis of the covalently linked nickel-pincer nucleotide (NPN) cofactor (pyridinium 3-thioamide-5-thiocarboxylic acid mononucleotide) of lactate racemase. Coenzyme A (CoA) stabilizes LarE and forms a CoA-Cys176 mixed disulfide with t ...
- Selmke, Benjamin; Borbat, Peter P.; Nickolaus, Chen; Varadarajan, Raghavan; Freed, Jack H.; Trommer, Wolfgang E.
- Biochemistry 2018 v.57 no.38 pp. 5507-5512
- X-radiation; active sites; binding proteins; crystal structure; electron paramagnetic resonance spectroscopy; ligands; maltose; molecular models; mutants; pH; prediction; protein folding
- ... An intensively investigated intermediate state of protein folding is the molten globule (MG) state, which contains secondary but hardly any tertiary structure. In previous work, we have determined the distances between interacting spins within maltose binding protein (MBP) in its native state using continuous wave and double electron–electron resonance (DEER) electron paramagnetic resonance (EPR) ...