... studies, and X-ray crystallography. The data show that the Trp triad stabilizes the folded V-domain by maintaining a short helix in the structure. Mutation of any Trp residue increases the structural plasticity of the domain. Residues Trp 61 and Trp 72 are involved in the binding of S100B, yet...

... Nitrogen assimilation Organosulfur degradation Sulfoacetaldehyde reductase X-ray crystallography Isethionate (Ise) is ubiquitous in the environment, and is also present in mammalian tissues [ 1 ]. There is no known pathway for isethionate biosynthesis in animals. Instead, it is thought...

... BY) . 3-aminopropionaldehyde 4-trimethylaminobutyraldehyde aldehyde dehydrogenase Homo sapiens structure-function X‐ray crystallography Aldehyde dehydrogenases (ALDHs) catalyze the NAD(P) + -dependent irreversible oxidation of aliphatic and aromatic aldehydes. To date, 24 ALDH gene families...

...# D2189). CRM197 Carrier Protein Conjugate Vaccine X-ray crystallography E. coli Reducing and nonreducing SDS/PAGE and Western blot analyses were performed with purified rCRM 197 as per the standard protocol [ 20 ]. Four micrograms of purified rCRM 197 along with the reference CRM...

... in a straightforward manner. Our study is a key example of how modern sulfur SAD combined with mutagenesis can help to advance and simplify the structural study of challenging coiled-coil domains by X-ray crystallography. All constructs were generated to have a 6x-His-tag and a thrombin cleavage site using...

... ( [email protected] ) * These authors contributed equally to this work. 16 01 2018 17 02 2018 22 02 2018 22 02 2018 covalent allostery high-throughput screen NMR spectroscopy protein-protein interactions X-ray crystallography Protein–protein interactions...

... Attribution Licence 3.0 . The polyphosphate kinase 2 (PPK2) from the intracellular pathogen Francisella tularensis has been characterized by a range of biochemical methods and X-ray crystallography. The antibiotic sensitivity of a deletion mutant lacking the gene encoding PPK2 is also reported...

... of mRNA. Here, we have used a combination of X-ray crystallography, RNA mutagenesis and site-specific cross-linking studies to investigate the molecular recognition of TS mRNA by the hTS enzyme. The interacting mRNA region was narrowed to the start codon and immediately flanking sequences. In the hTS...

...-site reactivity. enzyme kinetics enzyme structure NMR vitamins and cofactors X-ray crystallography Cobalamin, the biologically active form of vitamin B 12 , is an exquisitely complex natural product whose synthesis is limited to only some archaea and bacteria. It functions...

... conformational change pathogenic bacterium SDR enzyme UDP–sugar X–ray crystallography Staphylococcus aureus is normally a harmless commensal bacterium residing in 25% of the adult population, yet is a dangerous human pathogen in susceptible individuals [ 1 , 2 ]. S. aureus is also notorious...

... work is properly cited. auto-inactivation catalytic loop chimaera C-terminal domain glutamic acid decarboxylase X-ray crystallography GAD (glutamic acid decarboxylase) is a PLP (pyridoxal-5′-phosphate)-dependent enzyme that catalyses the α-decarboxylation of l -glutamate...

... ATPase calcium structure X-ray crystallography Bioscience Reports, Vol. 15, No. 5, 1995 REVIEW The Structure and Interactions of Ca2+-ATPase Anthony N. Martonosi Received September 14, 1995 Electron crystallographic studies on membrane crystals of Ca2+-ATPase reveal different patterns of ATPase...

...Robert Huber Aspects of intramolecular light energy and electron transfer will be discussed for three protein cofactor complexes, whose three-dimensional structures have been elucidated by x-ray crystallography: Components of light harvesting cyanobacterial phycobilisomes, the purple bacterial...