User:Tommie Hata/Introduction to Protein Engineering-Subtilisin
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<applet load='2sic' size='400' frame='true' align='right' caption='PDB ID 2sic, Subtilisin BPN' scene='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Default-whole/1'/> | <applet load='2sic' size='400' frame='true' align='right' caption='PDB ID 2sic, Subtilisin BPN' scene='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Default-whole/1'/> | ||
| - | The enzyme to the right is subtilisin BPN' from PDB file 2sic. The | + | The enzyme to the right is subtilisin BPN' from PDB file 2sic. The subtilisin enzyme is colored white while the ''Streptomyces'' subtilisin inhibitor is colored yellow. By <scene name='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Default/2'>minimizing the inhibitor to a fragment that is bound in the subtilisin active site</scene>, we can take a look at how the substrate binds the active site. Enzyme-inhibitor structures are more offen solved and deposited in the Protein Data Bank (PDB)compared to enzyme-substrate structures. This is because enzyme-substrate complexes are often transient by nature. Without being able to form a stable enzyme-substrate complex, crystals of the complex cannot be grown so that the structure can be solved through x-ray crystallography. |
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| + | , which has been minimized in the view to highlight the chain bound in the active site of subtilisin. | ||
<scene name='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Default/2'>TextToBeDisplayed</scene> | <scene name='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Default/2'>TextToBeDisplayed</scene> | ||
Revision as of 14:38, 6 August 2009
This Protein Engineering module has been developed using material from Dr. Scott Banta's course, Protein Engineering (chemical engineering department at Columbia University).
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The enzyme to the right is subtilisin BPN' from PDB file 2sic. The subtilisin enzyme is colored white while the Streptomyces subtilisin inhibitor is colored yellow. By , we can take a look at how the substrate binds the active site. Enzyme-inhibitor structures are more offen solved and deposited in the Protein Data Bank (PDB)compared to enzyme-substrate structures. This is because enzyme-substrate complexes are often transient by nature. Without being able to form a stable enzyme-substrate complex, crystals of the complex cannot be grown so that the structure can be solved through x-ray crystallography.
, which has been minimized in the view to highlight the chain bound in the active site of subtilisin.
Reference
- Takeuchi Y, Satow Y, Nakamura KT, Mitsui Y. Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. J Mol Biol. 1991 Sep 5;221(1):309-25. PMID:1920411
