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 FtsA forms actin-like protofilaments. FtsA forms actin-like protofilaments. EMBO J. (0261-4189) 2012 imex curation Szwedziak P., Wang Q., Freund SM., Löwe J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Szwedziak P., Wang Q., Freund SM., Löwe J. EMBO J. (0261-4189) 2012 Only protein-protein interactions imex curation FtsA forms actin-like protofilaments. FtsA forms actin-like protofilaments. EMBO J. (0261-4189) 2012 imex curation Szwedziak P., Wang Q., Freund SM., Löwe J. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati weight by comassie molecular weight estimation by coomasie staining weight by comassie Szwedziak P., Wang Q., Freund SM., Löwe J. EMBO J. (0261-4189) 2012 Only protein-protein interactions imex curation FtsA forms actin-like protofilaments. FtsA forms actin-like protofilaments. EMBO J. (0261-4189) 2012 imex curation Szwedziak P., Wang Q., Freund SM., Löwe J. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Szwedziak P., Wang Q., Freund SM., Löwe J. EMBO J. (0261-4189) 2012 Only protein-protein interactions imex curation FtsA forms actin-like protofilaments. FtsA forms actin-like protofilaments. EMBO J. (0261-4189) 2012 imex curation Szwedziak P., Wang Q., Freund SM., Löwe J. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Szwedziak P., Wang Q., Freund SM., Löwe J. EMBO J. (0261-4189) 2012 Only protein-protein interactions imex curation FtsA forms actin-like protofilaments. FtsA forms actin-like protofilaments. EMBO J. (0261-4189) 2012 imex curation Szwedziak P., Wang Q., Freund SM., Löwe J. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Szwedziak P., Wang Q., Freund SM., Löwe J. EMBO J. (0261-4189) 2012 Only protein-protein interactions imex curation ftsz_thema Cell division protein FtsZ ftsZ TM_0836 protein protein thema Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) MGFDLDVEKKKENRNIPQANNLKIKVIGVGGAGNNAINRMIEIGIHGVEFVAVNTDLQVLEASNADVKIQIGENITRGLGAGGRPEIGEQAALESEEKIREVLQDTHMVFITAGFGGGTGTGASPVIAKIAKEMGILTVAIVTTPFYFEGPERLKKAIEGLKKLRKHVDTLIKISNNKLMEELPRDVKIKDAFLKADETLHQGVKGISELITKRGYINLDFADIESVMKDAGAAILGIGVGKGEHRAREAAKKAMESKLIEHPVENASSIVFNITAPSNIRMEEVHEAAMIIRQNSSEDADVKFGLIFDDEVPDDEIRVIFIATRFPDEDKILFPEGDIPAIYRYGLEGLL mint 5F2E11FDAA92AFE7 q9wzu0_thema Cell division protein FtsA ftsA TM_0835 protein protein thema Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) MIDLSKTVFYTSIDIGSRYIKGLVLGKRDQEWEALAFSSVKSRGLDEGEIKDAIAFKESVNTLLKELEEQLQKSLRSDFVISFSSVSFEREDTVIERDFGEEKRSITLDILSEMQSEALEKLKENGKTPLHIFSKRYLLDDERIVFNPLDMKASKIAIEYTSIVVPLKVYEMFYNFLQDTVKSPFQLKSSLVSTAEGVLTTPEKDRGVVVVNLGYNFTGLIAYKNGVPIKISYVPVGMKHVIKDVSAVLDTSFEESERLIITHGNAVYNDLKEEEIQYRGLDGNTIKTTTAKKLSVIIHARLREIMSKSKKFFREVEAKIVEEGEIGIPGGVVLTGGGAKIPRINELATEVFKSPVRTGCYANSDRPSIINADEVANDPSFAAAFGNVFAVSENPYEETPVKSENPLKKIFRLFKELME mint 3A41B479596B4927 q9wzu0 5 FtsA 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint Furthermore, when co-crystallized with ATPgS, TmFtsA produced another crystal form containing continuous protofilaments that closely resemble the previous dimer and are again actin-like (Table I, Figure 3A and Supplementary Figure 5). t1 f3a sf5 PDB code: 4A2B ftsz-q9wzu0 5 FtsA 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified FtsZ 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-7808349]C-terminal positions must always be equal to the length of the protein sequence. Actual positions : 336-336, sequence length 351 [EBI-7808349]336-351 direct interaction direct interaction mint t1 f2 sf2 PDB code: 4A2A ftsz-q9wzu0-1 2 FtsA 7 weight by comassie molecular weight estimation by coomasie staining weight by comassie predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified FtsZ 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-7808392]C-terminal positions must always be equal to the length of the protein sequence. Actual positions : 344-344, sequence length 351 [EBI-7808392]344-351 direct interaction direct interaction mint f1b f1d ftsz-q9wzu0-2 1 FtsA 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified FtsZ 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-7808491]C-terminal positions must always be equal to the length of the protein sequence. Actual positions : 336-336, sequence length 351 [EBI-7808491]336-351 direct interaction direct interaction sf1 mint ftsz-q9wzu0-3 3 FtsA 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified FtsZ 6 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-7808543]C-terminal positions must always be equal to the length of the protein sequence. Actual positions : 336-336, sequence length 351 [EBI-7808543]336-351 direct interaction direct interaction sf4 mint q9wzu0-q9wzu0 4 FtsA 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified FtsA 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint f3c f3d We then took advantage of FtsA s affinity for membranes through polymerization on a lipid monolayer (Figure 3C and D). By using this technique we revealed several hundred nanometre long filaments, often present as doublets or higher-order structures. Interestingly, no exogenous nucleotide was required to obtain these, but it is important to note that the protein contains some bound ATP carried over from the purification, as is evident from the ATP in the crystal structure, which was not added. Occasionally, two-dimensional sheets were observed (Figure 3D). Fourier transformations of sheets (Figure 3D, top right) revealed a longitudinal spacing of around 48A° , corresponding to the spacing found in the crystal. This implies that the TmFtsA polymers visualized by electron microscopy and seen in atomic detail in the crystal structures are very similar or identical.