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Rip1 and PdtaR mutant transcriptional responses to Nitric oxide
- Description
BioProject Summary: "Analysis of the transcriptional response of M. tuberculosis Erdman lacking the Rip1 protease, the PdtaR response regulator, or both, to the NO donor DETA-NO" Abstract summary: "Bacterial pathogens that infect phagocytic cells must deploy mechanisms that sense and neutralize host microbicidal effectors. For Mycobacterium tuberculosis, the causative agent of tuberculosis, these...
- Subject
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Mycobacterium tuberculosisTriazenes
- Access Rights
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Free to All
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Cryo-EM 3D map of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE: EMD-29912
- Authors
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Xiao, XianshaLi, Huilin
- Description
Description from EMDB: "The molecular chaperone DnaK is essential for viability of Mycobacterium tuberculosis (Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP by the nucleotide exchange factor GrpE. It has been unclear how GrpE couples DnaK's nucleotide exchange with substrate release. Here we report a cryo-EM analysis of GrpE bound to an intact Mtb DnaK,...
- Subject
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Mycobacterium tuberculosisNucleotidesProtein Folding
- Access Rights
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Free to All
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Cryo-EM 3D map of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE: EMD-29913
- Authors
-
Xiao, XianshaLi, Huilin
- Description
Description from EMDB: "The molecular chaperone DnaK is essential for viability of Mycobacterium tuberculosis (Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP by the nucleotide exchange factor GrpE. It has been unclear how GrpE couples DnaK's nucleotide exchange with substrate release. Here we report a cryo-EM analysis of GrpE bound to an intact Mtb DnaK,...
- Subject
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Mycobacterium tuberculosisNucleotidesProtein Folding
- Access Rights
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Free to All
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Cryo-EM 3D focused map of the Mycobacterium tuberculosis Hsp70 protein DnaK SBD domain: EMD-29914
- Authors
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Xiao, XianshaLi, Huilin
- Description
Description from EMDB: "The molecular chaperone DnaK is essential for viability of Mycobacterium tuberculosis (Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP by the nucleotide exchange factor GrpE. It has been unclear how GrpE couples DnaK's nucleotide exchange with substrate release. Here we report a cryo-EM analysis of GrpE bound to an intact Mtb DnaK,...
- Subject
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Mycobacterium tuberculosisNucleotidesProtein Folding
- Access Rights
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Free to All