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 Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH. Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH. FEBS Lett. (0014-5793) 2012 Suno R., Shimoyama M., Abe A., Shimamura T., Shimodate N., Watanabe YH., Akiyama Y., Yoshida M. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Suno R., Shimoyama M., Abe A., Shimamura T., Shimodate N., Watanabe YH., Akiyama Y., Yoshida M. FEBS Lett. (0014-5793) 2012 ftsh_ecoli ATP-dependent zinc metalloprotease FtsH ftsH hflB mrsC tolZ b3178 JW3145 std Cell division protease FtsH protein protein ecoli Escherichia coli (strain K12) MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNNDQVREARINGREINVTKKDSNRYTTYIPVQDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASNNSGDNGSPKAPRPVDEPRTPNPGNTMSEQLGDK DIP protein P0AAI3 original sequence version: 45 E24A753D8F486CA1 ftsh-1 1 FtsH 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 6.0 direct interaction direct interaction f2 mint We tested the stability of the FtsH mutant hexamers by gel-filtration analysis in the presence of ATP. The main peaks of all G448 mutants and wild-type protein appeared at the position equivalent to 580 kDa, which is the molecular mass of the hexamer (Fig. 2). This result shows that the mutations at G448 do not interfere with the assembly of FtsH into the hexamer