Hong, Xia Zang, Jianye White, Janice Wang, Chao Pan, Cheol-Ho Zhao, Rui Murphy, Robert C. Dai, Shaodong Henson, Peter Kappler, John W. Hagman, James Zhang, Gongyi 2024-01-20T18:34:45Z 2024-01-20T18:34:45Z 2021-09-04 2010-08-17 0027-8424 https://pubs.kist.re.kr/handle/201004/131171 JMJD6 is a Jumonji C domain-containing hydroxylase. JMJD6 binds alpha-ketoglutarate and iron and has been characterized as either a histone arginine demethylase or U2AF65 lysyl hydroxylase. Here, we describe the structures of JMJD6 with and without alpha-keto-glutarate, which revealed a novel substrate binding groove and two positively charged surfaces. The structures also contain a stack of aromatic residues located near the active center. The side chain of one residue within this stack assumed different conformations in the two structures. Interestingly, JMJD6 bound efficiently to single-stranded RNA, but not to single-stranded DNA, double-stranded RNA, or double-stranded DNA. These structural features and truncation analysis of JMJD6 suggest that JMJD6 may bind and modify single-stand RNA rather than the previously reported peptide substrates. English NATL ACAD SCIENCES PHOSPHATIDYLSERINE RECEPTOR OXIDATIVE DEMETHYLATION HISTONE DEMETHYLATION CRYSTAL-STRUCTURES STRUCTURAL BASIS NUCLEAR PROTEIN FAMILY ENGULFMENT MECHANISM Interaction of JMJD6 with single-stranded RNA Article 10.1073/pnas.1008832107 1 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.107, no.33, pp.14568 - 14572 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 107 33 14568 14572 scie scopus 000281287600012 2-s2.0-77957061888 Multidisciplinary Sciences Science & Technology - Other Topics Article PHOSPHATIDYLSERINE RECEPTOR OXIDATIVE DEMETHYLATION HISTONE DEMETHYLATION CRYSTAL-STRUCTURES STRUCTURAL BASIS NUCLEAR PROTEIN FAMILY ENGULFMENT MECHANISM RNA binding proteins RNA modification RNA splicing