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User:Tommie Hata/Introduction to Protein Engineering-Subtilisin
From Proteopedia
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.
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
