Literature summary for 3.4.19.13 extracted from

Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K.
Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate (2006), Proc. Natl. Acad. Sci. USA, 103, 6471-6476.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant T391A, unable to undergo autocatalytic processing, at 2.55 A resolution. Structural comparison of the precursor and mature protein demonstrates that the structures of the core regions in the two proteins are unchanged, with marked differences near the active site. In the precursor, the segment corresponding to the C-terminal region of the L-subunit occupies the site where the loop, residues 438-449, forms the lid of the gamma-glutamyl group-binding pocket in the mature enzyme. Upon cleavage of the N-terminal peptide bond of Thr391, the newly produced C-terminus, residues 375390, flips out, allowing the 438-449 segment to form the gamma-glutamyl group-binding pocket. A water molecule is located near the carbonyl carbon atom of Gln-390. The spatial arrangement around the water and Thr391 relative to the scissile peptide bond appears suitable for the initiation of autocatalytic processing	Escherichia coli

Crystallization (Comment)

Organism

mutant T391A, unable to undergo autocatalytic processing, at 2.55 A resolution. Structural comparison of the precursor and mature protein demonstrates that the structures of the core regions in the two proteins are unchanged, with marked differences near the active site. In the precursor, the segment corresponding to the C-terminal region of the L-subunit occupies the site where the loop, residues 438-449, forms the lid of the gamma-glutamyl group-binding pocket in the mature enzyme. Upon cleavage of the N-terminal peptide bond of Thr391, the newly produced C-terminus, residues 375390, flips out, allowing the 438-449 segment to form the gamma-glutamyl group-binding pocket. A water molecule is located near the carbonyl carbon atom of Gln-390. The spatial arrangement around the water and Thr391 relative to the scissile peptide bond appears suitable for the initiation of autocatalytic processing

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
T391A	unable to undergo autocatalytic processing, crystallization data	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P18956	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	enzymes undergoes autocatalytic processing. Crystallization data	Escherichia coli

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Release 2023.1 (January 2023)