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Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.
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A Single-Point Mutation in d-Arginine Dehydrogenase Unlocks a Transient Conformational State Resulti
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Mechanism of the Clinically Relevant E305G Mutation in Human P450 CYP17A1
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Alteration of the O 2 -Producing Mn 4 Ca Cluster in Photosystem II by the Mutation of a Metal Ligand
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Pore Restructuring of Peptide Frameworks by Mutations at Distal Packing Residues
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Inactivating mutations and X-ray crystal structure of the tumor suppressor OPCML reveal cancer-associated functions
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Structure of DNMT3B homo-oligomer reveals vulnerability to impairment by ICF mutations
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Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies
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Distal mutations enhance catalysis in designed enzymes by facilitating substrate binding and product release
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Glioblastoma mutations alter EGFR dimer structure to prevent ligand bias
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Gene network analysis identifies dysregulated pathways in an autism spectrum disorder caused by mutations in Transcription Factor 4
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Effects of single and multiple nucleotide mutations on loop-mediated isothermal amplification
Nucleotide substitutions and deletions can slow or completely inhibit nucleic acid amplification compared to unmodified control samples.
Mutation of active site glutamate in serine hydroxymethyltransferase allows trapping a reactive intermediate: a combined neutron and X-ray crystallography study
Serine hydroxymethyltransferase (SHMT) is a pyridoxal-5′-phosphate (PLP) dependent enzyme that catalyzes a chemical transformation essential for the one-carbon (1C) metabolism. SHMT reversibly converts L-Ser into Gly and transfers a 1C unit to tetrahydrofolate (THF) to give 5,10-methylene-THF (5,10-MTHF). 5,10-MTHF, a 1C-unit donor, plays a crucial role in the downstream biomolecular syntheses required for the cell homeostasis and proliferation. SHMT is a prominent target for the drug discovery to battle bacterial and parasitic infections, and to treat various types of cancer. SHMT-catalyzed chemistry is governed by the general acid-base catalysis. Knowledge of the catalytic mechanism can aid drug design but can only be achieved when the atomic details of each reaction step are mapped, including accurate determination of hydrogen atom positions. Here we utilized the inactive E53Q mutant of Thermus thermophilus ( Tth ) SHMT to directly determine protonation states with room-temperature neutron crystallography and to capture a reactive intermediate containing the PLP-L-Ser external aldimine and THF in the enzyme active site. We observed protonation of the Schiff base nitrogen (N SB ) in the PLP internal aldimine but no change in the protonation states of other ionizable PLP groups and active site residues compared to wild-type Tth SHMT. X-ray structural analysis of the ternary intermediate complex E53Q-Ser-THF that eluded previous structural characterization shows the strategic positioning of the E53Q side chain in close proximity to the external aldimine and THF and reinforces the proposed role for E53 as the driver of proton transfer events along the reaction pathway.
Mutational fitness landscapes reveal genetic and structural improvement pathways for a vaccine-elici
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