3JTQ

Mutations in Cephalosporin Acylase Affecting Stability and Autoproteolysis

Summary for 3JTQ

• Entry DOI: 10.2210/pdb3jtq/pdb
• Related: 2ADV 2AE3 2AE4 3JTR
• Descriptor: Glutaryl 7-aminocephalosporanic acid acylase, GLYCEROL, ... (4 entities in total)
• Functional Keywords: cephalosporin acylase, autoproteolysis, hydrolase
• Biological source: Pseudomonas sp.; More
• Total number of polymer chains: 2
• Total formula weight: 77860.16

Authors

Cho, K.J.,Kim, J.K.,Lee, J.H.,Shin, H.J.,Park, S.S.,Kim, K.H. (deposition date: 2009-09-14, release date: 2010-01-26, Last modification date: 2023-11-01)

Primary citation

Cho, K.J.,Kim, J.K.,Lee, J.H.,Shin, H.J.,Park, S.S.,Kim, K.H.
Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.
Biochem.Biophys.Res.Commun., 390:342-348, 2009

PubMed Abstract: Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through two steps of intramolecular autoproteolysis, the first mediated by a serine residue, and the second by a glutamate, which releases the pro-segment and produces an active enzyme. In this study, we have determined the crystal structures of mutants which could affect primary or secondary auto-cleavage and of sequential intermediates of a slow-processing mutant at 2.0-2.5A resolutions. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt surprisingly different loop conformations from one another. However, the autoproteolytic site was found to form a catalytically competent conformation with a solvent water molecule, which was essentially conserved in the CA mutants.

PubMed: 19800869
DOI: 10.1016/j.bbrc.2009.09.134

Experimental method

X-RAY DIFFRACTION (2.2 Å)