Prp40: Difference between revisions
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<StructureSection load='1o6w' size='450' side='right' scene='Sandbox_504/Start_scene/1' caption=''> | <StructureSection load='1o6w' size='450' side='right' scene='Sandbox_504/Start_scene/1' caption='Yeast pre-mRNA processing protein Prp40 WW domain pair (PDB code [[1o6w]])'> | ||
== Structure of Prp40 == | == Structure of Prp40 == | ||
by Kelly Hrywkiw | by Kelly Hrywkiw | ||
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==The first FF domain (FF1)== | ==The first FF domain (FF1)== | ||
The <scene name='Sandbox_504/Start_scene_ff1/1'>FF1 domain of Prp40 is comprised of three alpha helices</scene>, and one 310 helix located between α2 and α3. Helices are composed of the following residues, <scene name='Sandbox_504/Ff1_a1/1'>α1</scene> (134-146), <scene name='Sandbox_504/Ff1_a2/2'>α2</scene> (154-163), <scene name='Sandbox_504/Ff1_310/1'>310</scene> (167-170), and <scene name='Sandbox_504/Ff1_a3/1'>α3</scene> (175-187). The core domain is made up of a series of aromatic and aliphatic residues. A type 1 β-turn is exhibited by the residues Asp149, Ser150, Thr151, and Trp152<ref name ="gasch"/>. | The <scene name='Sandbox_504/Start_scene_ff1/1'>FF1 domain of Prp40 is comprised of three alpha helices</scene>, and one 310 helix located between α2 and α3. Helices are composed of the following residues, <scene name='Sandbox_504/Ff1_a1/1'>α1</scene> (134-146), <scene name='Sandbox_504/Ff1_a2/2'>α2</scene> (154-163), <scene name='Sandbox_504/Ff1_310/1'>310</scene> (167-170), and <scene name='Sandbox_504/Ff1_a3/1'>α3</scene> (175-187). The core domain is made up of a series of aromatic and aliphatic residues. A type 1 β-turn is exhibited by the residues Asp149, Ser150, Thr151, and Trp152<ref name ="gasch"/>. | ||
==The fourth FF domain (FF4)== | ==The fourth FF domain (FF4)== | ||
<scene name='Sandbox_504/Start_scene_ff4/1'>Domain FF4 of Prp40</scene> exhibits compact four helical bundle fold comprised of an α1-α2-310-α3 topology. The composition of each helix is a follows <scene name='Sandbox_504/A1_of_ff4/1'>α1</scene> (Glu489-Thr507), <scene name='Sandbox_504/A2_of_ff4/1'>α2</scene> (Trp519-Leu526), <scene name='Sandbox_504/310_of_ff4/1'>310</scene> (Tyr532-Gly536) and <scene name='Sandbox_504/A3_of_ff4/1'>α3</scene> (Asp539-Phe549). There are a series of interactions between the different helices, for example Tyr532 is in contact with Phe500, Leu503, Ser523, and Arg542. A difference between FF1 and FF4 is the presence of five extra amino acids in F4 which gives the <scene name='Sandbox_504/Loop_of_ff4/1'>loop</scene> located between α 1 and α2 an extra turn. This insertion however does not increase the flexibility of F4 as compared to F1<ref name ="bonet"/>. | |||
</StructureSection> | |||
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Domain FF4 of Prp40 exhibits compact four helical bundle fold comprised of an α1-α2-310-α3 topology. The composition of each helix is a follows <scene name='Sandbox_504/A1_of_ff4/1'>α1</scene> (Glu489-Thr507), <scene name='Sandbox_504/A2_of_ff4/1'>α2</scene> (Trp519-Leu526), <scene name='Sandbox_504/310_of_ff4/1'>310</scene> (Tyr532-Gly536) and <scene name='Sandbox_504/A3_of_ff4/1'>α3</scene> (Asp539-Phe549). There are a series of interactions between the different helices, for example Tyr532 is in contact with Phe500, Leu503, Ser523, and Arg542. A difference between FF1 and FF4 is the presence of five extra amino acids in F4 which gives the <scene name='Sandbox_504/Loop_of_ff4/1'>loop</scene> located between α 1 and α2 an extra turn. This insertion however does not increase the flexibility of F4 as compared to F1<ref name ="bonet"/>. | |||
=Additional Resources= | =Additional Resources= | ||
*[http://www.rcsb.org/pdb/explore/explore.do?structureId=2KFD Prp40 FF4 domain, in the RCSB Protein Data Bank] | *[http://www.rcsb.org/pdb/explore/explore.do?structureId=2KFD Prp40 FF4 domain, in the RCSB Protein Data Bank] | ||