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 Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin. Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin. FEBS J. (1742-464X) 2012 Paul K., Chattopadhyay K. in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati weight by comassie molecular weight estimation by coomasie staining weight by comassie Paul K., Chattopadhyay K. FEBS J. (1742-464X) 2012 Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin. Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin. FEBS J. (1742-464X) 2012 Paul K., Chattopadhyay K. in vitro In vitro comigration in sds comigration in sds page comigration in sds weight by comassie molecular weight estimation by coomasie staining weight by comassie Paul K., Chattopadhyay K. FEBS J. (1742-464X) 2012 hlya_vibch Hemolysin hlyA VC_A0219 protein protein vibch Vibrio cholerae MPKLNRCAIAIFTILSAISSPTLLANINEPSGEAADIISQVADSHAIKYYNAADWQAEDNALPSLAELRDLVINQQKRVLVDFSQISDAEGQAEMQAQFRKAYGVGFANQFIVITEHKGELLFTPFDQAEEVDPQLLEAPRTARLLARSGFASPAPANSETNTLPHVAFYISVNRAISDEECTFNNSWLWKNEKGSRPFCKDANISLIYRVNLERSLQYGIVGSATPDAKIVRISLDDDSTGAGIHLNDQLGYRQFGASYTTLDAYFREWSTDAIAQDYRFVFNASNNKAQILKTFPVDNINEKFERKEVSGFELGVTGGVEVSGDGPKAKLEARASYTQSRWLTYNTQDYRIERNAKNAQAVSFTWNRQQYATAESLLNRSTDALWVNTYPVDVNRISPLSYASFVPKMDVIYKASATETGSTDFIIDSSVNIRPIYNGAYKHYYVVGAHQSYHGFEDTPRRRITKSASFTVDWDHPVFTGGRPVNLQLASFNNRCIQVDAQGRLAANTCDSQQSAQSFIYDQLGRYVSASNTKLCLDGEALDALQPCNQNLTQRWEWRKGTDELTNVYSGESLGHDKQTGELGLYASSNDAVSLRTITAYTDVFNAQESSPILGYTQGKMNQQRVGQDHRLYVRAGAAIDALGSASDLLVGGNGGSLSSVDLSGVKSITATSGDFQYGGQQLVALTFTYQDGRQQTVGSKAYVTNAHEDRFDLPAAAKITQLKIWSDDWLVKGVQFDLN C99FAE2A01F37CCE hlya-hlya-6 2 VCC 3 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 undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:50:51 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' Ala425Val VCC 3 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 undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:50:52 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' Ala425Val direct interaction direct interaction f4b mint We observed that a significantly reduced fraction of the Ala425Val-VCC mutant was converted into the SDS-stable oligomeric form as compared to the WT-VCC toxin, when incubated in presence of the Asolectin- cholesterol liposome (Fig. 4B). hlya-hlya-7 1 VCC 3 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 VCC 3 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 direct interaction direct interaction mint f4D Therefore, the Ala425Val mutation caused significant defect in the VCC toxin in terms of its binding, and not in terms its oligomerization ability, in the Asolectin-cholesterol liposome membrane. In this context, it is important to note that the interactions to the Asolectin liposome lacking cholesterol were drastically less for both the WT-VCC and Ala425Val-VCC molecules (Fig. 4C-D). Moreover, binding to the Asolectin liposome was comparable for both the wild type and the mutant variant (Fig. 4C-D).