Crystal Structure of the 47-kDa Lipoprotein of Treponema pallidum Reveals a Novel Penicillin-binding Protein
Open Access
- 1 November 2002
- journal article
- Published by Elsevier BV
- Vol. 277 (44), 41857-41864
- https://doi.org/10.1074/jbc.m207402200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Contributions of PBP 5 and dd -Carboxypeptidase Penicillin Binding Proteins to Maintenance of Cell Shape in Escherichia coliJournal of Bacteriology, 2001
- Complete Genome Sequence of Treponema pallidum , the Syphilis SpirocheteScience, 1998
- X-ray studies of enzymes that interact with penicillinsCellular and Molecular Life Sciences, 1998
- Kinship and Diversification of Bacterial Penicillin-Binding Proteins and β-LactamasesAntimicrobial Agents and Chemotherapy, 1998
- Treponema pallidum and the quest for outer membrane proteinsMolecular Microbiology, 1995
- The 47-kDa major lipoprotein immunogen of Treponema pallidum is a penicillin-binding protein with carboxypeptidase activity.Proceedings of the National Academy of Sciences of the United States of America, 1994
- SERINE β-LACTAMASES AND PENICILLIN-BINDING PROTEINSAnnual Review of Microbiology, 1991
- Bacterial Active-Site Serine Penicillin-Interactive Proteins and Domains: Mechanism, Structure, and EvolutionClinical Infectious Diseases, 1988
- Identification of Treponema pallidum penicillin-binding proteinsJournal of Bacteriology, 1987
- Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.Proceedings of the National Academy of Sciences of the United States of America, 1975