Literature: Glutamine synthetase, beta-Grasp domain (IPR008147)
References used in this entry
The following publications were referred to in the abstract:
Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCO.
Eisenberg D, Almassy RJ, Janson CA, Chapman MS, Suh SW, Cascio D, Smith WW.
Cold Spring Harb. Symp. Quant. Biol. 52 483-90 1987
PMID: 2900091 Related citations
Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold.
Burroughs AM, Balaji S, Iyer LM, Aravind L.
Biol. Direct 2 18 2007
PMID: 17605815 Related citations
Novel subunit-subunit interactions in the structure of glutamine synthetase.
Almassy RJ, Janson CA, Hamlin R, Xuong NH, Eisenberg D.
Nature 323 304-9 1986
PMID: 2876389 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition.
Gill HS, Eisenberg D.
Biochemistry 40 1903-12 2001
PMID: 11329256 Related citations
Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine.
Liaw SH, Pan C, Eisenberg D.
Proc. Natl. Acad. Sci. U.S.A. 90 4996-5000 1993
PMID: 8099447 Related citations
Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights.
Krajewski WW, Jones TA, Mowbray SL.
Proc. Natl. Acad. Sci. U.S.A. 102 10499-504 2005
PMID: 16027359 Related citations
Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium.
Liaw SH, Jun G, Eisenberg D.
Biochemistry 33 11184-8 1994
PMID: 7727369 Related citations
Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.
Gill HS, Pfluegl GM, Eisenberg D.
Biochemistry 41 9863-72 2002
PMID: 12146952 Related citations