THE CATALYTIC DOMAIN OF E. COLI LON PROTEASE HAS A UNIQUE FOLD AND A SER-LYS DYAD IN THE ACTIVE SITE
Journal Article
·
· Journal of Biological Chemistry
No abstract prepared.
- Research Organization:
- Brookhaven National Laboratory, National Synchrotron Light Source (US)
- Sponsoring Organization:
- DOE/OFFICE OF SCIENCE (US)
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 15015489
- Report Number(s):
- BNL-74278-2005-JA; JBCHA3; TRN: US200514%%52
- Journal Information:
- Journal of Biological Chemistry, Vol. 279; Other Information: PBD: 1 Jan 2004; ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- English
Similar Records
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad
Mutagenesis and Crystallographic Studies of the Catalytic Residues of the Papain Family Protease Bleomycin Hydrolase: New Insights into Active-site Structure
Crystal Structure of a Bacterial Signal Peptidase Apoenzyme. Implications for Signal Peptide Binding and the Ser-Lys Dyad Mechanism
Journal Article
·
Tue Dec 19 00:00:00 EST 2000
· Proc Natl Acad Sci USA
·
OSTI ID:15015489
Mutagenesis and Crystallographic Studies of the Catalytic Residues of the Papain Family Protease Bleomycin Hydrolase: New Insights into Active-site Structure
Journal Article
·
Mon Jan 01 00:00:00 EST 2007
· Biochemical Journal
·
OSTI ID:15015489
Crystal Structure of a Bacterial Signal Peptidase Apoenzyme. Implications for Signal Peptide Binding and the Ser-Lys Dyad Mechanism
Journal Article
·
Tue Jan 01 00:00:00 EST 2002
· J.Biol.Chem.277:9512,2002
·
OSTI ID:15015489