MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The role of the GAF and central domains of the transcriptional activator VnfA in Azotobacter vinelandii. The role of the GAF and central domains of the transcriptional activator VnfA in Azotobacter vinelandii. FEBS J. (1742-464X) 2011 imex curation Yoshimitsu K., Takatani N., Miura Y., Watanabe Y., Nakajima H. suggested by lperfetto 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 Yoshimitsu K., Takatani N., Miura Y., Watanabe Y., Nakajima H. suggested by lperfetto FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation vnfa_azovi Nitrogen fixation protein VnfA vnfA protein protein azovi Azotobacter vinelandii MSSLPQYCECGLGECRTDVLPLLYEMSQIATESGDLSSIISILLRLMKRHMKVVRGMVTLYDRDSGSIVLHESFGLSPEEAGKGVYLLGEGIIGRVVETGQSIVVPCIRDEPAFLNRTGSRDRDSDDANLSFICVPILRGRQVMGTISAERLYDNAELLKLDVEVLSILATTTAQAVELYLVENVENVALEAENRRLRSALGERFKPANIIGNSKPMLEVYQLIERVVRTRTTVLILGESGVGKELVAGAIHYNSPAAKGPFVKFNCASLPESVIESELFGHEKGSFTGAIGLRKGRFEEAAGGTIFLDEVGEMSLTTQAKLLRVLQERSFERVGGNTTIHVDLRVIAATNRNLAEMVADGTFAEDLYYRLNVFPITIPPLRERGSDIITLADHFVSRFSREMGIEVNRISTPRLNMLQSYQWPGNVRELENVIERAMLLSEDGVIHGYHLPPSLQAPVVGDSEAPPDGLEARLGAIEYELIVEALKLHHGNMTEAATHLGLTARVLGLRMGKYNLNYKDYR mint 35619FD910AF59A1 vnfa 1 VnfA 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:37:49 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' 35-177 Stoichiometry: 3.0 direct interaction direct interaction mint sf2c vnfa-1 1 VnfA 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction mint sf2a sf2b In size exclusion chromatography (SEC), ΔGAFVnfA showed a single elution peak corresponding to a molecular weight of 140 kDa, in agreement with a homotetrameric configuration of the ΔGAFVnfA monomer (36 kDa, calculated from the amino acid sequence) (Fig. S2A). As described in the previous report, the wild type took a tetrameric conformation in both the apo- and holo-forms [17]. The result, therefore, indicated that ΔGAFVnfA retained a quaternary structure similar to that of the wild type. The GAFVnfA showed two elution maxima when subjected to SEC, assignable to the tetrameric and octameric oligomers of the GAFVnfA monomer (23 kDa, Fig. S2B). A fraction of the octameric GAFVnfA eluted as tetrameric and octameric fractions in SEC analysis, again, suggesting that the octamer consists of two tetramers, and that these oligomeric configurations are in equilibrium in solution. Thus, both the GAF and central domain are capable of forming tetrameric conformations independently, and conjugation of the GAF and central domains is not essential for the tetrameric conformation.