Results 51 to 60 of about 4,851 (193)
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
eLife, 2020 ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the E.
Xue Fei +6 more
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mBio, 2022 Despite having a highly reduced genome, Chlamydia trachomatis undergoes a complex developmental cycle in which the bacteria differentiate between the following two functionally and morphologically distinct forms: the infectious, nonreplicative elementary
Nicholas A. Wood +4 more
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Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori [PDF]
Journal of Biological Chemistry, 2003 ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N ...
Dong Young, Kim, Kyeong Kyu, Kim
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, 2022 Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a
Yumeng Zhang (3115050) +6 more
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mBio, 2020 Chlamydia trachomatis is an obligate intracellular bacterium that undergoes a complex developmental cycle in which the bacterium differentiates between two functionally and morphologically distinct forms, the elementary body (EB) and reticulate body (RB),
Nicholas A. Wood +5 more
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Frontiers in Molecular Biosciences, 2021 Staphylococcus aureus is a leading cause of bacterial infections world-wide. Staphylococcal infections are preferentially treated with β-lactam antibiotics, however, methicillin-resistant S. aureus (MRSA) strains have acquired resistance to this superior
Kristoffer T. Bæk +8 more
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Frontiers in Molecular Biosciences, 2017 The ClpXP protease is a highly conserved AAA+ degradation machine that is present throughout bacteria and in eukaryotic organelles. ClpXP is essential in some bacteria, such as Caulobacter crescentus, but dispensible in others, such as Escherichia coli ...
Robert H. Vass +3 more
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mBio, 2016 Lipoteichoic acid (LTA) is an important cell wall component of Gram-positive bacteria and a promising target for the development of vaccines and antimicrobial compounds against Staphylococcus aureus.
Kristoffer T. Bæk +10 more
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Nature Communications, 2023 AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently translocated
Alireza Ghanbarpour +8 more
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The ClpX chaperone modulates assembly of the tubulin‐like protein FtsZ [PDF]
Molecular Microbiology, 2005 SummaryAssembly of the tubulin‐like cytoskeletal protein FtsZ into a ring structure establishes the location of the nascent division site in prokaryotes. Factors that modulate FtsZ assembly are essential for ensuring the precise spatial and temporal regulation of cytokinesis.
Richard B, Weart +4 more
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