<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zaveri A</submitter><funding>Medical Research Council</funding><funding>DBT/Wellcome Trust India Alliance</funding><funding>Department of Biotechnology, Ministry of Science and Technology, India</funding><pagination>1231-1246</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8059089</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>120(7)</volume><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</pubmed_abstract><journal>Biophysical journal</journal><pubmed_title>Mycobacterial STAND adenylyl cyclases: The HTH domain binds DNA to form biocrystallized nucleoids.</pubmed_title><pmcid>PMC8059089</pmcid><funding_grant_id>MR/P028225/1</funding_grant_id><pubmed_authors>Bose A</pubmed_authors><pubmed_authors>Shenoy AR</pubmed_authors><pubmed_authors>Visweswariah SS</pubmed_authors><pubmed_authors>Sharma S</pubmed_authors><pubmed_authors>Zaveri A</pubmed_authors><pubmed_authors>Rajendran A</pubmed_authors><pubmed_authors>Biswas P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mycobacterial STAND adenylyl cyclases: The HTH domain binds DNA to form biocrystallized nucleoids.</name><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</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Apr</publication><modification>2026-05-31T06:03:26.112Z</modification><creation>2025-02-19T01:55:26.874Z</creation></dates><accession>S-EPMC8059089</accession><cross_references><pubmed>33217386</pubmed><doi>10.1016/j.bpj.2020.11.008</doi></cross_references></HashMap>