User:Tommie Hata/Introduction to Protein Engineering-Subtilisin: Difference between revisions
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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 structure to the right is subtilisin BPN' and streptomyces subtilisin inhibitor (PDB ID: [http://www.pdb.org/pdb/explore/explore.do?structureId=2SIC 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/3'>minimizing the inhibitor to a fragment that is bound in the subtilisin active site</scene>, we can take a look at | The structure to the right is subtilisin BPN' and streptomyces subtilisin inhibitor (PDB ID: [http://www.pdb.org/pdb/explore/explore.do?structureId=2SIC 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/3'>minimizing the inhibitor to a fragment that is bound in the subtilisin active site</scene>, we can take a closer look at the active site. Enzyme-inhibitor structures are common in the Protein Data Bank (PDB)compared to enzyme-substrate structures. This is because enzyme-substrate complexes are often transient. The inability to form a stable enzyme-substrate complex makes it difficult to grow a crystal for structural determination through X-ray crystallography. In comparison, enzyme inhibitors bind their targets with much higher affinity (low dissociation constant) which makes the enzyme-inhibitor complex more favorable to crystallize for structure determination. | ||
Subtilisin is a serine protease. The <scene name='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Labeled_active_site/1'>catalytic triad in the active site</scene> is made up of aspartic acid (Asp32), histidine (His64), and serine (Ser221). | Subtilisin is a serine protease. The <scene name='User:Tommie_Hata/Introduction_to_Protein_Engineering-Subtilisin/Labeled_active_site/1'>catalytic triad in the active site</scene> is made up of aspartic acid (Asp32), histidine (His64), and serine (Ser221). | ||
Revision as of 16:11, 18 September 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 structure to the right is subtilisin BPN' and streptomyces subtilisin inhibitor (PDB ID: 2sic). The subtilisin enzyme is colored white while the Streptomyces subtilisin inhibitor is colored yellow. By , we can take a closer look at the active site. Enzyme-inhibitor structures are common in the Protein Data Bank (PDB)compared to enzyme-substrate structures. This is because enzyme-substrate complexes are often transient. The inability to form a stable enzyme-substrate complex makes it difficult to grow a crystal for structural determination through X-ray crystallography. In comparison, enzyme inhibitors bind their targets with much higher affinity (low dissociation constant) which makes the enzyme-inhibitor complex more favorable to crystallize for structure determination.
Subtilisin is a serine protease. The is made up of aspartic acid (Asp32), histidine (His64), and serine (Ser221).
, which has been minimized in the view to highlight the chain bound in the active site of subtilisin.