Entry | Database: PDB / ID: 4u0g |
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Title | Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist |
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Components | - (ATP-dependent Clp protease proteolytic subunit ...) x 2
- ADEP-2B5Me
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Keywords | hydrolase/antibiotic / hydrolase / peptidase / hydrolase-antibiotic complex |
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Function / homology | Function and homology information
endopeptidase Clp / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / peptidoglycan-based cell wall / ATPase binding / serine-type endopeptidase activity / plasma membrane / cytosolSimilarity search - Function ClpP, Ser active site / Endopeptidase Clp serine active site. / ClpP, histidine active site / Endopeptidase Clp histidine active site. / ATP-dependent Clp protease proteolytic subunit / Clp protease proteolytic subunit /Translocation-enhancing protein TepA / Clp protease / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily ...ClpP, Ser active site / Endopeptidase Clp serine active site. / ClpP, histidine active site / Endopeptidase Clp histidine active site. / ATP-dependent Clp protease proteolytic subunit / Clp protease proteolytic subunit /Translocation-enhancing protein TepA / Clp protease / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily / Alpha-Beta Complex / Alpha BetaSimilarity search - Domain/homology ADEP-2B5Me / N-[(benzyloxy)carbonyl]-L-isoleucyl-L-leucine / ATP-dependent Clp protease proteolytic subunit 2 / ATP-dependent Clp protease proteolytic subunit 1Similarity search - Component |
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Biological species | ![](img/tx_bacteria.gif) Mycobacterium tuberculosis (bacteria) synthetic construct (others) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.1978 Å |
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Authors | Schmitz, K.R. / Carney, D.W. / Sello, J.K. / Sauer, R.T. |
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Funding support | United States, 1items Organization | Grant number | Country |
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National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | GM-101988 | United States |
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2014 Title: Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Authors: Schmitz, K.R. / Carney, D.W. / Sello, J.K. / Sauer, R.T. |
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History | Deposition | Jul 11, 2014 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Oct 8, 2014 | Provider: repository / Type: Initial release |
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Revision 1.1 | Oct 15, 2014 | Group: Database references |
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Revision 1.2 | Nov 12, 2014 | Group: Database references |
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Revision 1.3 | Sep 6, 2017 | Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Other / Refinement description / Source and taxonomy Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_audit_support / pdbx_database_status / pdbx_entity_src_syn / pdbx_struct_oper_list / software Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_entity_src_syn.pdbx_alt_source_flag / _pdbx_struct_oper_list.symmetry_operation |
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Revision 1.4 | Dec 25, 2019 | Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization |
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Revision 2.0 | Nov 15, 2023 | Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Refinement description Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_validate_peptide_omega / pdbx_validate_torsion / refine_hist / struct_conn / struct_ncs_dom_lim Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_label_atom_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id |
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