Entry | Database: PDB / ID: 5ts0 |
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Title | Structure of Mycobacterium tuberculosis proteasome in complex with N,C-capped dipeptide PKS2208 |
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Components | - Proteasome subunit alpha
- Proteasome subunit beta
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Keywords | HYDRONLASE/HYDROLASE inhibitor / N / C-capped dipeptides / Mycobacterium tuberculosis / proteasome / inhibitors / HYDRONLASE-HYDROLASE inhibitor complex |
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Function / homology | Function and homology information
symbiont-mediated perturbation of host defenses / zymogen binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasomal protein catabolic process / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / peptidoglycan-based cell wall / proteolysis involved in protein catabolic process / modification-dependent protein catabolic process ...symbiont-mediated perturbation of host defenses / zymogen binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasomal protein catabolic process / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / peptidoglycan-based cell wall / proteolysis involved in protein catabolic process / modification-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / extracellular region / plasma membrane / cytoplasm / cytosolSimilarity search - Function Proteasome, alpha subunit, bacterial / Proteasome subunit beta, actinobacteria / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta ...Proteasome, alpha subunit, bacterial / Proteasome subunit beta, actinobacteria / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha BetaSimilarity search - Domain/homology (2S)-N-{(2S)-3-methoxy-1-[(naphthalen-1-ylmethyl)amino]-1-oxopropan-2-yl}-4-oxo-2-[(3-phenylpropanoyl)amino]-4-(1H-pyrrol-1-yl)butanamide (non-preferred name) / Chem-7J1 / Proteasome subunit alpha / Proteasome subunit beta / Proteasome subunit beta / Proteasome subunit alphaSimilarity search - Component |
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Biological species | ![](img/tx_bacteria.gif) Mycobacterium tuberculosis (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.84679745871 Å |
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Authors | Hsu, H.-C. / Fan, H. / Singh, P.K. / Wang, R. / Sukenick, G. / Nathan, C. / Lin, G. / Li, H. |
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Funding support | United States, 1items Organization | Grant number | Country |
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National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) | R01 AI070285 | United States |
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Citation | Journal: Biochemistry / Year: 2017 Title: Structural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome. Authors: Hsu, H.C. / Singh, P.K. / Fan, H. / Wang, R. / Sukenick, G. / Nathan, C. / Lin, G. / Li, H. |
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History | Deposition | Oct 27, 2016 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jan 11, 2017 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jan 18, 2017 | Group: Database references |
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Revision 1.2 | Sep 27, 2017 | Group: Author supporting evidence / Refinement description / Category: pdbx_audit_support / software Item: _pdbx_audit_support.funding_organization / _software.name |
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Revision 1.3 | Dec 11, 2019 | Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization |
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Revision 1.4 | Mar 6, 2024 | Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession |
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