Sandbox108

Glutamine synthetase assignment by UMBC undergraduate students

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Ligands:	ADP, CL, MN, P3S
Gene:	GLUL, GLNS (Homo sapiens)
Activity:	Glutamate--ammonia ligase, with EC number 6.3.1.2
Related:	2ojw
Structural annotation: Resources: InterPro : Ipr014746, Ipr008147, Ipr008146 Pfam : PF00120, PF03951 UniProt : P15104
Functional annotation: Cellular component: cytoplasm Biological process: nitrogen compound metabolic process glutamine biosynthetic process regulation of neurotransmitter levels Molecular function: ligase activity 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, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Exercise 2 Exercise 3 Exercise 4 Exercise 4(Practiced)

OUTLINE

Tertiary Structure

Different groups of amino acids specify a variety of properties of their side chains. In general, there are five categories; non-polar and aliphatic R groups, aromatic R groups, polar and uncharged R groups, positively charged R groups, and negatively charged R groups.

Glutamine is within uncharged polar <show the uncharged polar groups wiki text>. Usually, uncharged polar groups are classified as hydrophilic that is found on the outside of proteins <show the hydrophilic wiki text>. Also, amino acids with the character of acidic or basic side chains are polar, showing on the outside of molecules <show the polar wiki text>. Glutamine has no side chain on non-polar group, but the side chain on non-polar groups of the proteins usually tends to be hydrophobic <show the hydrophobic of cysteine wiki text> and to cluster together inside.[1]

Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain. [2] Hydrophobic interaction is a major driving force determining the tertiary structure of the proteins. [3] The reason why hydrophobic interaction is important is because of relationship with the hydrogen bonding. The peptide backbone is hydrophilic, but in the middle of proteins is mostly in a hydrophobic circumstance. So, in order to reduce the hydrophilicity, to maximize the hydrogen bonding, the α-helix <show α-helix wiki text> and the β-sheet <show the β-sheet wiki text> can break down the C=O and N-H groups in the peptide bonds so that the hydrogen bonds are maximum. [4] Also, all polar and hydrophilic side chains interact with H-bonds. Hydrogen bonding <show the H.B wiki text> is crucial in stabilizing the tertiary structure. [5] On the other hand, disulfide bonds <show the disulfide bonds of cysteine wiki text> between cysteine residues stabilize the tertiary structure. [6]