Ann Taylor Sandbox 111': Difference between revisions
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==Succinyl-AAPR-trypsin acyl-enzyme== | ==Succinyl-AAPR-trypsin acyl-enzyme== | ||
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction | |||
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Revision as of 16:45, 18 February 2011
Succinyl-AAPR-trypsin acyl-enzymeSuccinyl-AAPR-trypsin acyl-enzyme
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction
Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure.
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| 2age, resolution 1.15Å () | |||||||||
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| Ligands: | |||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||
| Related: | 2agg, 2agi, 2ah4
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
