The structure of the nicotinamide-adenine dinucleotide coenzyme when bound to lactate dehydrogenase.
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Animals↗
Biomedical subjects
R W Schevitz
Publications and source records attributed to R W Schevitz.
Low resolution study of crystalline L-lactate dehydrogenase.
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Animals↗
The three-dimensional structure of trp repressor.
The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure near the DNA binding surface.
Bacterial Proteins↗
The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.
Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking alpha-helices from both subunits.
Apoproteins↗