Sandbox Reserved 983
From Proteopedia
(Difference between revisions)
Line 4: | Line 4: | ||
To understand the mechanisms of tryptophan synthase, the structure of the enzyme must first be studied. The general form of the enzyme is an α2β2 complex in which the α subunit forms a TIM barrel and the β subunit has a type II fold conformation.<ref>"Tryptophan Synthase." - Proteopedia, Life in 3D. Web. 26 Jan. 2015. <http://www.proteopedia.org/wiki/index.php/Tryptophan_synthase>. | To understand the mechanisms of tryptophan synthase, the structure of the enzyme must first be studied. The general form of the enzyme is an α2β2 complex in which the α subunit forms a TIM barrel and the β subunit has a type II fold conformation.<ref>"Tryptophan Synthase." - Proteopedia, Life in 3D. Web. 26 Jan. 2015. <http://www.proteopedia.org/wiki/index.php/Tryptophan_synthase>. | ||
- | <references/></ref> Additionally, the enzyme has two binding sites: an indole 3-glycerol binding site and an indole and serine binding site. Another important feature that allows for the tryptophan synthase to perform its function is its hydrophobic channel which makes it possible for indoles to diffuse to the appropriate site instead of diffusing out to cell’s cytosol.<ref>Nelson, David L., and Michael M. Cox. Lehninger Principles of Biochemistry. 6th ed. New York: W.H. Freeman, 2013. Print.</ref> | + | <references/></ref> Additionally, the enzyme has two binding sites: an indole 3-glycerol binding site and an indole and serine binding site. Another important feature that allows for the tryptophan synthase to perform its function is its hydrophobic channel which makes it possible for indoles to diffuse to the appropriate site instead of diffusing out to cell’s cytosol.<ref>Nelson, David L., and Michael M. Cox. Lehninger Principles of Biochemistry. 6th ed. New York: W.H. Freeman, 2013. Print.</ref> |
== Function == | == Function == | ||
Line 14: | Line 14: | ||
== Structural highlights == | == Structural highlights == | ||
The structure of Tryptophan Synthase is in an alpha-beta-beta-alpha complex with two binding sites: an indole 3-glycerol binding site and an indole and serine binding site. | The structure of Tryptophan Synthase is in an alpha-beta-beta-alpha complex with two binding sites: an indole 3-glycerol binding site and an indole and serine binding site. | ||
- | |||
- | <scene name='68/687333/Alpha_subunit/2'>α Subunit</scene> | ||
Revision as of 14:12, 9 April 2015
This Sandbox is Reserved from 15-Jan-2015, through 30-May-2015 for use in the course "Biochemistry" taught by Jason Telford at the Maryville University. This reservation includes Sandbox Reserved 977 through Sandbox Reserved 986. |
To get started:
More help: Help:Editing |
Tryptophan Synthase
|
References
1. Dunn, Michael F., Dimitri Niks, Huu Ngo, Thomas R.m. Barends, and Ilme Schlichting. "Tryptophan Synthase: The Workings of a Channeling Nanomachine."Trends in Biochemical Sciences 33.6 (2008): 254-64. Science Direct. Web. 25 Jan. 2015. <http://www.sciencedirect.com/science/article/pii/S0968000408000923>.
2. "Tryptophan Synthase." - Proteopedia, Life in 3D. Web. 26 Jan. 2015. <http://www.proteopedia.org/wiki/index.php/Tryptophan_synthase>.
- ↑ "Tryptophan Synthase." - Proteopedia, Life in 3D. Web. 26 Jan. 2015. <http://www.proteopedia.org/wiki/index.php/Tryptophan_synthase>. <references/>
- ↑ Nelson, David L., and Michael M. Cox. Lehninger Principles of Biochemistry. 6th ed. New York: W.H. Freeman, 2013. Print.
3. Nelson, David L., and Michael M. Cox. Lehninger Principles of Biochemistry. 6th ed. New York: W.H. Freeman, 2013. Print.