2AH4

guanidinobenzoyl-trypsin acyl-enzyme at 1.13 A resolution

Summary for 2AH4

• Entry DOI: 10.2210/pdb2ah4/pdb
• Related: 2AGE 2AGG 2AGI
• Descriptor: beta-trypsin, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: acyl-enzyme; serine protease; proteinase; peptidase; hydrolase, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 1
• Total formula weight: 23927.79

Authors

Radisky, E.S.,Lee, J.M.,Lu, C.J.,Koshland Jr., D.E. (deposition date: 2005-07-26, release date: 2006-05-16, Last modification date: 2024-10-16)

Primary citation

Radisky, E.S.,Lee, J.M.,Lu, C.J.,Koshland Jr., D.E.
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates
Proc.Natl.Acad.Sci.USA, 103:6835-6840, 2006

PubMed Abstract: 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 this classic 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.

PubMed: 16636277
DOI: 10.1073/pnas.0601910103

Experimental method

X-RAY DIFFRACTION (1.13 Å)