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Glutamine synthetase assignment by UMBC undergraduate studentsGlutamine synthetase assignment by UMBC undergraduate students

spinqualitylabelsall models PDB ID 2gls Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2gls, resolution 3.50Å ()
Ligands:
Activity:	Glutamate--ammonia ligase, with EC number 6.3.1.2
Structural annotation: Resources: CATH : 2Glsa02, 2Glsa01, 2Glsb02, 2Glsb01, 2Glsc01, 2Glsc02, 2Glsd02, 2Glsd01, 2Glse02, 2Glse01, 2Glsf02, 2Glsf01, 2Glsg01, 2Glsg02, 2Glsh02, 2Glsh01, 2Glsi02, 2Glsi01, 2Glsj01, 2Glsj02, 2Glsk01, 2Glsk02, 2Glsl02, 2Glsl01 InterPro : Ipr014746, Ipr008146, Ipr001637, Ipr008147, Ipr004809 Pfam : PF00120, PF03951 SCOP : d2glsa2, d2glsa1, d2glsb2, d2glsb1, d2glsc1, d2glsc2, d2glsd2, d2glsd1, d2glse2, d2glse1, d2glsf1, d2glsf2, d2glsg2, d2glsg1, d2glsh2, d2glsh1, d2glsi2, d2glsi1, d2glsj2, d2glsj1, d2glsk1, d2glsk2, d2glsl2, d2glsl1 UniProt : P0A1P6
Functional annotation: Cellular component: cytoplasm Biological process: nitrogen compound metabolic process glutamine biosynthetic process nitrogen fixation Molecular function: ligase activity nucleotide binding glutamate-ammonia ligase activity catalytic activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Glutamine synthetase of Salmonella typhimurium

Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain [1] and mostly affected by () interaction and hydrogen bonding. In general, hydrophobic interaction is a major driving force determining the most tertiary structure of the proteins. Hydrogen bonding is crucial in stabilizing the tertiary structure as well.[2] Also, disulfide bonds stabilize the tertiary structure in residues such as cysteine residues.[3] However, for Salmonella typhimurium it is mostly influenced by the helix-helix interactions between 12-subunits enzymes within two layers.[4]

Glutamine synthetase from Salmonella typhimurium is the 12-subunits enzyme, and has 23 helix-helix interactions involving helices of chain A with four different types of interactions. [5] The 12-subunits enzyme are arranged in two layers of six, such as which is the one of the protein residues of Salmonella typhimurium; at the interface of pairs of subunits within each layer, six anti-parallel beta strands formed cylindrical active sites.[6] Each active site holds two ions surrounded by some [7] Also, the protein ligands to Mn2+ 469 are , , and ; those to Mn2+ 470 are , , and .[8] Glutamine from Salmonella typhimurium has 12-subunits of each of them in pairs within two layers. COOH terminus and a helical thong, which inserts into a pocket formed by two neighboring subunits on the opposite ring, hold the two layers of subunits tightly.[9] Also, can affect the form of tertiary structure, but interactions will contribute to the stability of the intersubunit between two layers more efficiently.[10] In the other hand, the most effective interaction in glutamine synthetase from Salmonella typhimurium is the helix-helix interactions. The folding of the proteins can be affected by the 12-subunits in the residues. In the case of Salmonella typhimurium the helices of chain A has , while most glutamine has uncharged side chain which formed by replacing the hydroxyl of glutamic acid with an amine functional group.

As a result, the only helix-helix interactions will be the most powerful sources of being in the glutamine synthetase of Salmonella typhimurium.