DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology 2016 imex curation Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. DIP original experiment: DIP-268853X Nature structural & molecular biology 2016 IMEx The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology 2016 imex curation Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. DIP original experiment: DIP-268852X Nature structural & molecular biology 2016 IMEx The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology 2016 imex curation Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. DIP original experiment: DIP-268848X Nature structural & molecular biology 2016 IMEx The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology 2016 imex curation Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. DIP original experiment: DIP-268850X Nature structural & molecular biology 2016 IMEx The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology 2016 imex curation Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. DIP original experiment: DIP-268851X Nature structural & molecular biology 2016 IMEx The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology 2016 imex curation Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Mulligan C., Fenollar-Ferrer C., Fitzgerald GA., Vergara-Jaque A., Kaufmann D., Li Y., Forrest LR., Mindell JA. DIP original experiment: DIP-268849X Nature structural & molecular biology 2016 IMEx The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. q9kne0_vibch VC_A0025 protein protein vibch Vibrio cholerae MNRNDSVPLPTNTREWFLHRNSLIVLADVALFLALYHFLPFEHNVVLGISMLAFIAVLWLTEALHVTVTAILVPVMAVFFGIFETQAALNNFANSIIFLFLGGFALAAAMHHQGLDKVIADKVLAMAQGKMSVAVFMLFGVTALLSMWISNTATAAMMLPLVLGVLSKVDADKQRSTYVFVLLGVAYSASIGGIATLVGSPPNAIAAAEVGLSFTDWMKFGLPTAMMMLPMAIAILYFLLKPTLNGMFELDRAPVNWDKGKVVTLGIFGLTVFLWIFSSPINAALGGFKSFDTLVALGAILMLSFARVVHWKEIQKTADWGVLLLFGGGLCLSNVLKQTGTSVFLANALSDMVSHMGIFVVILVVATFVVFLTEFASNTASAALLIPVFATVAEAFGMSPVLLSVLIAVAASCAFMLPVATPPNAIVFASGHIKQSEMMRVGLYLNIACIGLLTAIAMLFWQ DIP protein Q9KNE0 original sequence version: 71 DIP protein Q9KNE0 original sequence version: 47 q9kne0_vibch-1 3 7 unspecified role unspecified role unspecified role unspecified role Q9KNE0:p.[Val68Cys;Ser304Cys] V68C/S304C mutation mutation certain certain sequence position certain certain certain sequence position certain V C certain certain sequence position certain certain certain sequence position certain S C This feature has been corrected as a result of our quality control procedures. The original label was 'V68C/S304C'. Wed May 02 17:09:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val68cys,ser304cys' Tue Jun 30 15:39:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Val68Cys;Ser304Cys]' ecolx Escherichia coli direct interaction direct interaction q9kne0_vibch-2 5 7 unspecified role unspecified role unspecified role unspecified role Q9KNE0:p.Lys316Cys K316C mutation mutation certain certain sequence position certain certain certain sequence position certain K C This feature has been corrected as a result of our quality control procedures. The original label was 'K316C'. Wed May 02 20:16:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys316cys' Tue Jun 30 18:47:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys316Cys' ecolx Escherichia coli direct interaction direct interaction q9kne0_vibch-3 2 7 unspecified role unspecified role unspecified role unspecified role Q9KNE0:p.Val364Cys V364C mutation mutation certain certain sequence position certain certain certain sequence position certain V C This feature has been corrected as a result of our quality control procedures. The original label was 'V364C'. Wed May 02 15:05:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val364cys' Tue Jun 30 16:58:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val364Cys' ecolx Escherichia coli direct interaction direct interaction q9kne0_vibch-4 6 7 unspecified role unspecified role unspecified role unspecified role Q9KNE0:p.[Gln86Cys;Ser95Cys] Q86C/S95C mutation mutation certain certain sequence position certain certain certain sequence position certain S C certain certain sequence position certain certain certain sequence position certain Q C This feature has been corrected as a result of our quality control procedures. The original label was 'Q86C/S95C'. Wed May 02 15:17:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln86cys,ser95cys' Tue Jun 30 17:01:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gln86Cys;Ser95Cys]' ecolx Escherichia coli direct interaction direct interaction q9kne0_vibch-5 4 7 unspecified role unspecified role unspecified role unspecified role Q9KNE0:p.Asn90Cys N90C mutation mutation certain certain sequence position certain certain certain sequence position certain N C This feature has been corrected as a result of our quality control procedures. The original label was 'N90C'. Wed May 02 17:55:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn90cys' Tue Jun 30 20:18:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn90Cys' ecolx Escherichia coli direct interaction direct interaction q9kne0_vibch-6 1 7 unspecified role unspecified role unspecified role unspecified role Q9KNE0:p.Val165Cys V165C mutation mutation certain certain sequence position certain certain certain sequence position certain V C This feature has been corrected as a result of our quality control procedures. The original label was 'V165C'. Wed May 02 19:38:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val165cys' Tue Jun 30 16:57:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val165Cys' ecolx Escherichia coli direct interaction direct interaction