{"doi":"10.1021/bi0272508","title":"A Spring-Loaded State of NusG in Its Functional Cycle Is Suggested by X-ray Crystallography and Supported by Site-Directed Mutants","abstract":null,"journal":"Biochemistry","year":2003,"id":676829,"datarank":0.5955437870328184,"base_score":3.970291913552122,"endowment":3.970291913552122,"self_citation_contribution":0.5955437870328184,"citation_network_contribution":0.0,"self_endowment_contribution":0.5955437870328184,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":52,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1068668,"name":"Mikhail Bubunenko","orcid":"0009-0004-7906-9488","position":1,"is_corresponding":false},{"id":1768413,"name":"Michelle Andrykovitch","orcid":null,"position":2,"is_corresponding":false},{"id":1378462,"name":"Wei Guo","orcid":"0000-0003-3634-0077","position":3,"is_corresponding":false},{"id":1768418,"name":"Karen M. Routzahn","orcid":null,"position":4,"is_corresponding":false},{"id":589375,"name":"David S. Waugh","orcid":"0000-0003-0776-8488","position":5,"is_corresponding":false},{"id":372754,"name":"Donald L. Court","orcid":null,"position":6,"is_corresponding":false},{"id":514836,"name":"Xinhua Ji","orcid":"0000-0001-6942-1514","position":7,"is_corresponding":false},{"id":1768406,"name":"J. Randy Knowlton","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A Spring-Loaded State of NusG in Its Functional Cycle Is Suggested by X-ray Crystallography and Supported by Site-Directed Mutants","abstract":"Transcription factor NusG is present in all prokaryotes, and orthologous proteins have also been identified in yeast and humans. NusG contains a 27-residue KOW motif, found in ribosomal protein L24 where it interacts with rRNA. NusG in Escherichia coli (EcNusG) is an essential protein and functions as a regulator of Rho-dependent transcription termination, phage lambda N and rRNA transcription antitermination, and phage HK022 Nun termination. Relative to EcNusG, Aquifex aeolicus NusG (AaNusG) and several other bacterial NusG proteins contain a variable insertion sequence of approximately 70 residues in the central region of the molecule. Recently, crystal structures of AaNusG in space groups P2(1) and I222 have been reported; the authors conclude that there are no conserved dimers among the contacting molecules in the crystals [Steiner, T., Kaiser, J. T., Marinkovic, S., Huber, R., and Wahl, M. C. (2002) EMBO J. 21, 4641-4653]. We have independently determined the structures of AaNusG also in two crystal forms, P2(1) and C222(1), and surprisingly found that AaNusG molecules form domain-swapped dimers in both crystals. Additionally, polymerization is also observed in the P2(1) crystal. A unique \"ball-and-socket\" junction dominates the intermolecular interactions within both oligomers. We believe that this interaction is a clue to the function of the molecule and propose a spring-loaded state in the functional cycle of NusG. The importance of the ball-and-socket junction for the function of NusG is supported by the functional analysis of site-directed mutants.","is_dataset_classified":null,"base_score":3.970291913552122,"endowment":3.970291913552122,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"12600194","pmcid":null,"openalex_id":"https://openalex.org/W2085755086","authors":[],"funders":[],"total_grants":0,"fwci":0.6841,"citation_percentile":0.67508435,"influential_citations":0,"citation_trend":[{"year":2012,"count":4},{"year":2013,"count":3},{"year":2014,"count":2},{"year":2015,"count":2},{"year":2016,"count":2},{"year":2017,"count":2},{"year":2018,"count":2},{"year":2019,"count":1},{"year":2020,"count":1},{"year":2021,"count":2},{"year":2024,"count":2},{"year":2026,"count":1}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://pubs.acs.org/doi/pdf/10.1021/bi0272508","host_type":"publisher"},{"url":"https://doi.org/10.1021/bi0272508","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/12600194","host_type":"repository"}],"fields_of_study":["RNA and protein synthesis mechanisms","Bacterial Genetics and Biotechnology","Bacteriophages and microbial interactions"],"mesh_terms":["Amino Acid Sequence","Bacterial Proteins","Molecular Sequence Data","Peptide Elongation Factors","Phenylalanine","Structure-Activity Relationship","Transcription Factors","Mutagenesis, Site-Directed","Protein Structure, Tertiary","Crystallography, X-Ray","Dimerization","Amino Acid Substitution","Escherichia coli Proteins"],"keywords":["Crystallography","Biology","Aquifex aeolicus","Escherichia coli","Stereochemistry","Chemistry","Biochemistry","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T03:10:11.828880Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}