2PKC

CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION

Summary for 2PKC

• Entry DOI: 10.2210/pdb2pkc/pdb
• Descriptor: PROTEINASE K, SODIUM ION (3 entities in total)
• Functional Keywords: hydrolase(serine proteinase)
• Biological source: Engyodontium album
• Total number of polymer chains: 1
• Total formula weight: 28953.77

Authors

Mueller, A.,Hinrichs, W.,Wolf, W.M.,Saenger, W. (deposition date: 1993-06-04, release date: 1994-01-31, Last modification date: 2024-10-16)

Primary citation

Muller, A.,Hinrichs, W.,Wolf, W.M.,Saenger, W.
Crystal structure of calcium-free proteinase K at 1.5-A resolution.
J.Biol.Chem., 269:23108-23111, 1994

PubMed Abstract: Proteinase K from the fungus Tritirachium album Limber binds two Ca2+ ions, one strongly (Ca 1) and the other weakly (Ca 2). Removal of these cations reduces the stability of proteinase K as shown by thermal denaturation, but the proteolytic activity is unchanged. The x-ray structures of native and Ca(2+)-free proteinase K at 1.5-A resolution show that there are no cuts in the polypeptide backbone (i.e. no autolysis), Ca 1 has been replaced by Na+, while Ca 2 has been substituted by a water associated with a larger but locally confined structural change at that site. A small but concerted geometrical shift is transmitted from the Ca 1 site via eight secondary structure elements to the substrate recognition site (Gly100-Tyr104, and Ser132-Gly136) but not to the catalytic triad (Asp39,His69,Ser224). This is accompanied by positional changes of localized waters.

PubMed: 8083213

Experimental method

X-RAY DIFFRACTION (1.5 Å)