Entry | Database: PDB / ID: 3mmp |
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Title | Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins |
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Components | - Elongation factor Tu 2, Elongation factor Ts
- RNA-directed RNA polymerase beta chain
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Keywords | TRANSFERASE / RdRp / host-factor complex / translation |
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Function / homology | Function and homology information
guanyl-nucleotide exchange factor complex / translational elongation / guanosine tetraphosphate binding / translation elongation factor activity / guanyl-nucleotide exchange factor activity / RNA-directed RNA polymerase / viral RNA genome replication / response to antibiotic / RNA-dependent RNA polymerase activity / nucleotide binding ...guanyl-nucleotide exchange factor complex / translational elongation / guanosine tetraphosphate binding / translation elongation factor activity / guanyl-nucleotide exchange factor activity / RNA-directed RNA polymerase / viral RNA genome replication / response to antibiotic / RNA-dependent RNA polymerase activity / nucleotide binding / GTPase activity / GTP binding / RNA binding / zinc ion binding / membrane / metal ion binding / plasma membrane / cytoplasm / cytosolSimilarity search - Function RNA-directed RNA polymerase beta-chain / RNA replicase, beta-chain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / RNA-directed RNA polymerase, bacteriophage, catalytic domain ...RNA-directed RNA polymerase beta-chain / RNA replicase, beta-chain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / RNA-directed RNA polymerase, bacteriophage, catalytic domain / RdRp of RNA-containing bacteriophages catalytic domain profile. / Ubiquitin-associated (UBA) domain / Translation elongation factor EFTu/EF1A, bacterial/organelle / Elongation factor Tu, domain 2 / Elongation factor Tu (EF-Tu), GTP-binding domain / Translation elongation factor EFTu/EF1A, C-terminal / Elongation factor Tu C-terminal domain / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / UBA-like superfamily / Translation factors / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Elongation Factor Tu (Ef-tu); domain 3 / Helicase, Ruva Protein; domain 3 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / DNA/RNA polymerase superfamily / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha BetaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_bacteria.gif) Escherichia coli (E. coli)
Enterobacteria phage Qbeta (virus) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å |
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Authors | Kidmose, R.T. / Vasiliev, N.N. / Chetverin, A.B. / Knudsen, C.R. / Andersen, G.R. |
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2010 Title: Structure of the Qbeta replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins. Authors: Kidmose, R.T. / Vasiliev, N.N. / Chetverin, A.B. / Andersen, G.R. / Knudsen, C.R. |
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History | Deposition | Apr 20, 2010 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jun 9, 2010 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 13, 2011 | Group: Version format compliance |
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Revision 1.2 | Jul 26, 2017 | Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software |
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Revision 1.3 | Sep 6, 2023 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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