Sandbox 16
From Proteopedia
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The <scene name='Sandbox_16/Alp-1/2'>secondary structure</scene> contains the double β-barrel motif (colored yellow) that is characteristic of the chymotrypsin family. The <scene name='Sandbox_16/Alp-1/3'>active site</scene> consists of Methionine 190, Methionine 213, and Valine 218 which are responsible for the specificity of the enzyme and its preference to cleave substrates on the C-terminal side of small hydrophobic residues, such as Alanine and Valine. | The <scene name='Sandbox_16/Alp-1/2'>secondary structure</scene> contains the double β-barrel motif (colored yellow) that is characteristic of the chymotrypsin family. The <scene name='Sandbox_16/Alp-1/3'>active site</scene> consists of Methionine 190, Methionine 213, and Valine 218 which are responsible for the specificity of the enzyme and its preference to cleave substrates on the C-terminal side of small hydrophobic residues, such as Alanine and Valine. | ||
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Revision as of 17:21, 22 June 2010
Alpha-lytic protease
Alpha-lytic protease (αlp) is a 198-aa extracellular bacterial serine protease produced by Lysobacter enzymogenes. The three-dimensional fold of αlp puts it in the same class as cymotrypsin, trypsin and other digestive serine proteases despite only modest sequence homology[1]. However, unlike its thermodynamically stable homologs, αlp is stabilized by a large unfolding activation barrier. This kinetic stability optimizes the native state to survive under the harsh, proteolytic conditions in which it operates. Since the native state is less stable than both an intermediate and a completely unfolded state, αlp requires a pro region to facilitate folding by stabilizing the folding transition state as well as the native state. After folding, the pro region is proteolytically cleaved, leaving an active αlp kinetically trapped
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| 2alp, resolution 1.70Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Alpha-lytic endopeptidase, with EC number 3.4.21.12 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Structure
The contains the double β-barrel motif (colored yellow) that is characteristic of the chymotrypsin family. The consists of Methionine 190, Methionine 213, and Valine 218 which are responsible for the specificity of the enzyme and its preference to cleave substrates on the C-terminal side of small hydrophobic residues, such as Alanine and Valine.
