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The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
Open accessAbstract
We have determined the crystal structure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 A resolution using an ab initio phasing procedure that exploits the internal 14-fold symmetry of the oligomer. The structure of a ClpP monomer has a distinct fold that defines a fifth structural family of serine proteases but a conserved catalytic apparatus. The active protease resembles a hollow, solid-walled cylinder composed of two 7-fold symmetric rings stacked back-to-back. Its 14 proteolytic active sites are located within a central, roughly spherical chamber approximately 51 A in diameter. Access to the proteolytic chamber is controlled by two axial pores, each having a minimum diameter of approximately 10 A. From the structural features of ClpP, we suggest a model for its action in degrading proteins.
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PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · cited 1×
“At 5 A ˚ resolution, the map proteins in the DALI database (Holm and Sander, 1993) showed some inconsistencies with the starting molecurevealed only a weak similarity between the threelar mask.”
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Cited by
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
Stress Physiology of Lactic Acid Bacteria.
Papadimitriou, K., Alegría, Á., Bron, P. A., de Angelis, M., Gobbetti, M., Kleerebezem, M., Lemos, J. A., Linares, D. M., Ross, P., Stanton, C., et al. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00076-15 · Cited by 914
Dysregulation of bacterial proteolytic machinery by a new class of antibiotics
Brötz-Oesterhelt, H., Beyer, D., Kroll, H.-P., Endermann, R., Ladel, C., Schroeder, W., Hinzen, B., Raddatz, S., Paulsen, H., Henninger, K., et al. (2005) · Nature Medicine · doi:10.1038/nm1306 · Cited by 505
Frees, D., Savijoki, K., Varmanen, P., & Ingmer, H. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05598.x · Cited by 288
Bacterial Proteases and Virulence
Frees, D., Brøndsted, L., & Ingmer, H. (2013) · Subcellular Biochemistry · doi:10.1007/978-94-007-5940-4_7 · Cited by 159
Metadata
- Authors
- Wang, J., Hartling, J. A., & Flanagan, J. M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-11
- Volume
- 91
- Issue
- 4
- Pages
- 447-456
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2145571109
- Cited by
- 591
- References
- 2
- FWCI
- 8.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Wang, J., Hartling, J. A., & Flanagan, J. M. (1997). The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis. Cell. https://doi.org/10.1016/s0092-8674(00)80431-6
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