{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zaveri A"],"funding":["Medical Research Council","DBT/Wellcome Trust India Alliance","Department of Biotechnology, Ministry of Science and Technology, India"],"pagination":["1231-1246"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8059089"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(7)"],"pubmed_abstract":["Mycobacteria harbor a unique class of adenylyl cyclases with a complex domain organization consisting of an N-terminal putative adenylyl cyclase domain fused to a nucleotide-binding adaptor shared by apoptotic protease-activating factor-1, plant resistance proteins, and CED-4 (NB-ARC) domain, a tetratricopeptide repeat (TPR) domain, and a C-terminal helix-turn-helix (HTH) domain. The products of the rv0891c-rv0890c genes represent a split gene pair, where Rv0891c has sequence similarity to adenylyl cyclases, and Rv0890c harbors the NB-ARC-TPR-HTH domains. Rv0891c had very low adenylyl cyclase activity so it could represent a pseudoenzyme. By analyzing the genomic locus, we could express and purify Rv0890c and find that the NB-ARC domain binds ATP and ADP, but does not hydrolyze these nucle"],"journal":["Biophysical journal"],"pubmed_title":["Mycobacterial STAND adenylyl cyclases: The HTH domain binds DNA to form biocrystallized nucleoids."],"pmcid":["PMC8059089"],"funding_grant_id":["MR/P028225/1"],"pubmed_authors":["Bose A","Shenoy AR","Visweswariah SS","Sharma S","Zaveri A","Rajendran A","Biswas P"],"additional_accession":[]},"is_claimable":false,"name":"Mycobacterial STAND adenylyl cyclases: The HTH domain binds DNA to form biocrystallized nucleoids.","description":"Mycobacteria harbor a unique class of adenylyl cyclases with a complex domain organization consisting of an N-terminal putative adenylyl cyclase domain fused to a nucleotide-binding adaptor shared by apoptotic protease-activating factor-1, plant resistance proteins, and CED-4 (NB-ARC) domain, a tetratricopeptide repeat (TPR) domain, and a C-terminal helix-turn-helix (HTH) domain. The products of the rv0891c-rv0890c genes represent a split gene pair, where Rv0891c has sequence similarity to adenylyl cyclases, and Rv0890c harbors the NB-ARC-TPR-HTH domains. Rv0891c had very low adenylyl cyclase activity so it could represent a pseudoenzyme. By analyzing the genomic locus, we could express and purify Rv0890c and find that the NB-ARC domain binds ATP and ADP, but does not hydrolyze these nucle","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-05-31T06:03:26.112Z","creation":"2025-02-19T01:55:26.874Z"},"accession":"S-EPMC8059089","cross_references":{"pubmed":["33217386"],"doi":["10.1016/j.bpj.2020.11.008"]}}