{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T03:40:59Z","timestamp":1760240459487,"version":"build-2065373602"},"reference-count":62,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2019,6,21]],"date-time":"2019-06-21T00:00:00Z","timestamp":1561075200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["105440; 494213"],"award-info":[{"award-number":["105440; 494213"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>The C3-like toxins are single-domain proteins that represent a minimal mono-ADP-ribosyl transferase (mART) enzyme with a simple model scaffold for the entire cholera toxin (CT)-group. These proteins possess a single (A-domain) that modifies Rho proteins. In contrast, C2-like toxins require a binding\/translocation partner (B-component) for intoxication. These are A-only toxins that contain the E-x-E motif, modify G-actin, but are two-domains with a C-domain possessing enzymatic activity. The N-domain of the C2-like toxins is unstructured, and its function is currently unknown. A sequence-structure-function comparison was performed on the N-terminal region of the mART domain of the enzymatic component of the CT toxin group in the CATCH fold (3.90.210.10). Special consideration was given to the N-domain distal segment, the \u03b1-lobe (\u03b11\u2013\u03b14), and its different roles in these toxin sub-groups. These results show that the role of the N-terminal \u03b1-lobe is to provide a suitable configuration (i) of the \u03b12\u2013\u03b13 helices to feature the \u03b13-motif that has a role in NAD+ substrate binding and possibly in the interaction with the protein target; (ii) the \u03b13\u2013\u03b14 helices to provide the \u03b13\/4-loop with protein-protein interaction capability; and (iii) the \u03b11-Ntail that features specialized motif(s) according to the toxin type (A-only or A-B toxins) exhibiting an effect on the catalytic activity via the ARTT-loop, with a role in the inter-domain stability, and with a function in the binding and\/or translocation steps during the internalization process.<\/jats:p>","DOI":"10.3390\/toxins11060365","type":"journal-article","created":{"date-parts":[[2019,6,21]],"date-time":"2019-06-21T11:54:31Z","timestamp":1561118071000},"page":"365","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["An In-Silico Sequence-Structure-Function Analysis of the N-Terminal Lobe in CT Group Bacterial ADP-Ribosyltransferase Toxins"],"prefix":"10.3390","volume":"11","author":[{"given":"Miguel R.","family":"Lugo","sequence":"first","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph N1G 2W1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8559-8384","authenticated-orcid":false,"given":"A. Rod","family":"Merrill","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph N1G 2W1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2019,6,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1038\/nrmicro3310","article-title":"Novel bacterial ADP-ribosylating toxins: Structure and function","volume":"12","author":"Simon","year":"2014","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1.26.1","DOI":"10.1002\/0471250953.bi0126s49","article-title":"Investigating protein structure and evolution with SCOP2","volume":"49","author":"Andreeva","year":"2015","journal-title":"Curr. Protoc. 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