Structural highlights
Function
[DHE4_ECOLI] Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.[1] [2]
Publication Abstract from PubMed
Structural biology and structural genomics projects routinely rely on recombinantly expressed proteins, but many proteins and complexes are difficult to obtain by this approach. We investigated native source proteins for high-throughput protein crystallography applications. The Escherichia coli proteome was fractionated, purified, crystallized, and structurally characterized. Macro-scale fermentation and fractionation were used to subdivide the soluble proteome into 408 unique fractions of which 295 fractions yielded crystals in microfluidic crystallization chips. Of the 295 crystals, 152 were selected for optimization, diffraction screening, and data collection. Twenty-three structures were determined, four of which were novel. This study demonstrates the utility of native source proteins for high-throughput crystallography.
Macro-to-Micro Structural Proteomics: Native Source Proteins for High-Throughput Crystallization.,Totir M, Echols N, Nanao M, Gee CL, Moskaleva A, Gradia S, Iavarone AT, Berger JM, May AP, Zubieta C, Alber T PLoS One. 2012;7(2):e32498. Epub 2012 Feb 29. PMID:22393408[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Veronese FM, Boccu E, Conventi L. Glutamate dehydrogenase from Escherichia coli: induction, purification and properties of the enzyme. Biochim Biophys Acta. 1975 Feb 19;377(2):217-28. PMID:235298
- ↑ Sakamoto N, Kotre AM, Savageau MA. Glutamate dehydrogenase from Escherichia coli: purification and properties. J Bacteriol. 1975 Nov;124(2):775-83. PMID:241744
- ↑ Totir M, Echols N, Nanao M, Gee CL, Moskaleva A, Gradia S, Iavarone AT, Berger JM, May AP, Zubieta C, Alber T. Macro-to-Micro Structural Proteomics: Native Source Proteins for High-Throughput Crystallization. PLoS One. 2012;7(2):e32498. Epub 2012 Feb 29. PMID:22393408 doi:10.1371/journal.pone.0032498
