User:Uzoma Anele

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Uzoma Anele, Sandeep Pulugurtha Undergraduate students at the University of Maryland, Baltimore County.

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Contents 1 Exercise 1 2 Exercise 2 3 Exercise 3 4 Exercise 4 5 Outline 6 References

Exercise 1

spinqualitylabelsall models Glutamine Synthetase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Exercise 2

Exercise 3

Exercise 4

Outline

Helical thongs provide a significant amount of intersubunit stabilization to the quaternary structure of glutamine synthetase by binding together subunits from the two layers. A typical is composed of a nonpolar carboxyl terminus that inserts into a hydrophobic compartment created by two adjoining subunits on the opposite, corresponding layer. Thirty-seven of the 77 residues of which the helical thong and hydrophobic pocket consist, are apolar and involved in the direct contact between the helical thong and pocket. These residues contain an atypical abundance of proline and valine, 16% and 10%, respectively. This unusual amount may serve to enhance its rigidity and cohesion.

spinqualitylabelsall models Helical Thong of Glutamine Synthetase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

References

1. Eisenberg, D., et.al., Structure-function relationships of glutamine synthetases, Biochim Biophys Acta 2000: 1477, 122-145.

2. Yamashita, M. M., et.al., Refined Atolnic Model of Glutamine Synthetase at 3.5 A Resolution, J Biol Chem 1989 264: 17681-17690.