Self-activation by a C-terminal domain arginine finger regulates GTP hydrolysis in bacterial zinc metallochaperones.

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Bibliographic Details
Title: Self-activation by a C-terminal domain arginine finger regulates GTP hydrolysis in bacterial zinc metallochaperones.
Authors: Rocchio JS; Department of Chemistry, Indiana University, Bloomington, IN 47405., Osterberg MK; Department of Chemistry, Indiana University, Bloomington, IN 47405., McRae EM; Department of Chemistry, Indiana University, Bloomington, IN 47405., Jaiswal N; Department of Chemistry, Indiana University, Bloomington, IN 47405., Edmonds KA; Department of Chemistry, Indiana University, Bloomington, IN 47405., Doyle DA; Department of Pathology, Microbiology, and Immunology, and Vanderbilt Institute for Infection, Immunology, and Inflammation, Vanderbilt University Medical Center, Nashville, TN 37232., Skaar EP; Department of Pathology, Microbiology, and Immunology, and Vanderbilt Institute for Infection, Immunology, and Inflammation, Vanderbilt University Medical Center, Nashville, TN 37232., Giedroc DP; Department of Chemistry, Indiana University, Bloomington, IN 47405.
Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2026 Jun 09; Vol. 123 (23), pp. e2608072123. Date of Electronic Publication: 2026 Jun 02.
Publication Type: Journal Article
Journal Info: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
Database: MEDLINE Ultimate
Description
ISSN:1091-6490
DOI:10.1073/pnas.2608072123