DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993) 2010 imex curation Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. DIP original experiment: DIP-217189X Structure (London, England : 1993) 2010 IMEx Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993) 2010 imex curation Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. DIP original experiment: DIP-217191X Structure (London, England : 1993) 2010 IMEx Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993) 2010 imex curation Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. DIP original experiment: DIP-217190X Structure (London, England : 1993) 2010 IMEx Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993) 2010 imex curation Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. DIP original experiment: DIP-217188X Structure (London, England : 1993) 2010 IMEx Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993) 2010 imex curation Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. DIP original experiment: DIP-217192X Structure (London, England : 1993) 2010 IMEx Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993) 2010 imex curation Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Chen B., Sysoeva TA., Chowdhury S., Guo L., De Carlo S., Hanson JA., Yang H., Nixon BT. DIP original experiment: DIP-217187X Structure (London, England : 1993) 2010 IMEx Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. b5xst9_klep3 RNA polymerase sigma-54 factor rpoN KPK_0509 protein protein klep3 Klebsiella pneumoniae (strain 342) MKQGLQLRLSQQLAMTPQLQQAIRLLQLSTLELQQELQQALESNPLLEQTDLHDEVEAKEVEDRESLDTVDALEQKEMPDELPLDASWDEIYTAGTPSGNGVDYQDDELPVYQGETTQTLQDYLMWQVELTPFTDTDRAIATSIVDAVDDTGYLTIQIEDIVDSIGDDEIGLEEVEAVLKRIQRFDPVGVAAKDLRDCLLIQLSQFAKETPWLEEARLIISDHLDLLANHDFRTLMRVTRLKEEVLKEAVNLIQSLDPRPGQSIHTSEPEYVIPDVLVRKVSGRWTVELNADSIPRLKINQQYAAMGNSARNDADGQFIRSNLQEARWLIKSLESRNDTLLRVSRCIVEQQQAFFEQGEEYMKPMVLADIAQAVEMHESTISRVTTQKYLHSPRGIFELKYFFSSHVNTEGGGEASSTAIRALVKKLIAAENPAKPLSDSKLTSMLSEQGIMVARRTVAKYRESLSIPPSNQRKQLV DIP protein B5XST9 original sequence version: 13 o67198_aquae ntrC1 aq_1117 protein protein aquae Aquifex aeolicus (strain VF5) MNVLVIEDDKVFRGLLEEYLSMKGIKVESAERGKEAYKLLSEKHFNVVLLDLLLPDVNGLEILKWIKERSPETEVIVITGHGTIKTAVEAMKMGAYDFLTKPCMLEEIELTINKAIEHRKLRKENELLRREKDLKEEEYVFESPKMKEILEKIKKISCAECPVLITGESGVGKEVVARLIHKLSDRSKEPFVALNVASIPRDIFEAELFGYEKGAFTGAVSSKEGFFELADGGTLFLDEIGELSLEAQAKLLRVIESGKFYRLGGRKEIEVNVRILAATNRNIKELVKEGKFREDLYYRLGVIEIEIPPLRERKEDIIPLANHFLKKFSRKYAKEVEGFTKSAQELLLSYPWYGNVRELKNVIERAVLFSEGKFIDRGELSCLVNSKGIKNKHKSIKEIEKEEIIKVLKEVNFNKKLASEILGIPLRTLYRRLKEYGIE AAE1E9780271DFC0 ntrc1-1 6 8 unspecified role unspecified role unspecified role unspecified role Central domain Region 121-387 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ntrc1-rpon-1 3 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Central domain Region 121-387 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain O67198:p.Arg299Ala R299A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R299A'. Wed May 02 14:53:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg299ala' Tue Jun 30 17:24:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg299Ala' ecolx Escherichia coli direct interaction direct interaction ntrc1-2 4 8 unspecified role unspecified role unspecified role unspecified role Central domain Region 121-387 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ntrc1-3 2 8 unspecified role unspecified role unspecified role unspecified role Central domain Region 121-387 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ntrc1-4 1 8 unspecified role unspecified role unspecified role unspecified role Central domain Region 121-387 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ntrc1-rpon-2 5 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Central domain Region 121-387 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction