Glutamine synthetase
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Glutamine Synthetase
Structure
An unrefined structure of glutamine synthetase is made of two layers, each containing 6 subunits, for a total of 12 subunits. [1] Each subunit contains an which is defined by a cylindrical shape formed by six antiparalel β starnds contributed by one subunit and two more strands by the neighbouring subunit. [1] In each cylindrical active site there are two Mn2+ ions: Mn 2+ 469 and 470. Both are attached to three protein chains and two water molecules, one of the water molecules are shared by both Mn2+. The protein ligands. Attached to Mn 2+ 469 is: Glu-131, GLu-212 and Glu-220, and the protein ligands attached to Mn 2+ are: Glu-129, His-269 and Glu-357.[1]
Unique to glutamine synthetase, unlike other enzymes, is it's "passive site". This refers to the central loop which is formed by a segment of the backbone that extends into the central aqueous cavity. [1]Unlike other sites in glutamine synthetase under the same conditions, this site is suceptible to proteolysis by four secreated proteases from the V8 protease of Staphylococcus aureus.[1]
Classes
Glutamine synthetase has been described as having three destinctive types.[2]
- Class I (GSI): Genes for this class have only been found in bacteria (eubacteria) and archaea (arhaebacteria. The paper by Kumada et. al goes into detail on these two.[2]
- Class II (GSII): Genes for this class have only been found in eukaryotes and a few soil-dwelling bacteria.The paper by Kumada again, gets into further detail about these bacteria.[2]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Yamashita MM, Almassy RJ, Janson CA, Cascio D, Eisenberg D. Refined atomic model of glutamine synthetase at 3.5 A resolution. J Biol Chem. 1989 Oct 25;264(30):17681-90. PMID:2572586
- ↑ 2.0 2.1 2.2 Brown JR, Masuchi Y, Robb FT, Doolittle WF. Evolutionary relationships of bacterial and archaeal glutamine synthetase genes. J Mol Evol. 1994 Jun;38(6):566-76. PMID:7916055
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