Entry Database : PDB / ID : 6duq Structure visualization Downloads & linksTitle Structure of a Rho-NusG KOW domain complex Components(Transcription ...) x 2 rU12 DetailsKeywords TRANSCRIPTION/RNA / Rho / NusG / RecA / ATPase / TRANSCRIPTION / TRANSCRIPTION-RNA complexFunction / homology Function and homology informationFunction Domain/homology Component
DNA-templated transcription elongation / ATP-dependent activity, acting on RNA / transcription elongation-coupled chromatin remodeling / transcription elongation factor complex / regulation of DNA-templated transcription elongation / helicase activity / transcription antitermination / DNA-templated transcription termination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ribosome biogenesis ... DNA-templated transcription elongation / ATP-dependent activity, acting on RNA / transcription elongation-coupled chromatin remodeling / transcription elongation factor complex / regulation of DNA-templated transcription elongation / helicase activity / transcription antitermination / DNA-templated transcription termination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ribosome biogenesis / hydrolase activity / ATP hydrolysis activity / RNA binding / ATP binding / identical protein binding / membrane / cytosol Similarity search - Function Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / : ... Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / : / Transcription antitermination protein, NusG / Transcription antitermination protein, NusG, bacteria, conserved site / Transcription termination factor nusG signature. / Cold shock domain / Cold shock protein domain / NusG-like / Transcription termination factor nusG / NusG, N-terminal / In Spt5p, this domain may confer affinity for Spt4p. It possesses a RNP-like fold. / NusG, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / KOW (Kyprides, Ouzounis, Woese) motif. / Translation protein SH3-like domain superfamily / KOW motif / KOW / Ribosomal protein L2, domain 2 / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homology ADENOSINE-5'-DIPHOSPHATE / BERYLLIUM TRIFLUORIDE ION / RNA / RNA (> 10) / Transcription termination/antitermination protein NusG / Transcription termination factor Rho / Transcription termination/antitermination protein NusG / Transcription termination factor Rho Similarity search - ComponentBiological species Escherichia coli M718 (bacteria)Escherichia coli M605 (bacteria)synthetic construct (others) Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 3.7 Å DetailsAuthors Berger, J.M. / Lawson, M.R. Funding support United States, 2items Details Hide detailsOrganization Grant number Country National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) GM071747 United States Other private G. Harold and Leila Y. Mathers Foundation United States
CitationJournal : Mol. Cell / Year : 2018Title : Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.Authors : Lawson, M.R. / Ma, W. / Bellecourt, M.J. / Artsimovitch, I. / Martin, A. / Landick, R. / Schulten, K. / Berger, J.M. History Deposition Jun 21, 2018 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Sep 5, 2018 Provider : repository / Type : Initial releaseRevision 1.1 Oct 3, 2018 Group : Data collection / Database references / Category : citationItem : _citation.journal_volume / _citation.page_first / _citation.page_lastRevision 1.2 Apr 17, 2019 Group : Author supporting evidence / Data collection / Category : pdbx_audit_support / Item : _pdbx_audit_support.funding_organizationRevision 1.3 Jan 1, 2020 Group : Author supporting evidence / Category : pdbx_audit_support / Item : _pdbx_audit_support.funding_organizationRevision 1.4 Jan 29, 2020 Group : Derived calculations / Category : pdbx_struct_assembly_gen / Item : _pdbx_struct_assembly_gen.asym_id_listRevision 1.5 Mar 13, 2024 Group : Data collection / Database references / Derived calculationsCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
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