4QNX

Crystal structure of apo-CmoB

4QNX の概要

• エントリーDOI: 10.2210/pdb4qnx/pdb
• 関連するPDBエントリー: 4QNU 4QNV
• 分子名称: tRNA (mo5U34)-methyltransferase, SULFATE ION (3 entities in total)
• 機能のキーワード: structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, rossmann fold, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75641.98

構造登録者

Kim, J.,Toro, R.,Bhosle, R.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC) (登録日: 2014-06-18, 公開日: 2014-09-17, 最終更新日: 2024-02-28)

主引用文献

Kim, J.,Xiao, H.,Koh, J.,Wang, Y.,Bonanno, J.B.,Thomas, K.,Babbitt, P.C.,Brown, S.,Lee, Y.S.,Almo, S.C.
Determinants of the CmoB carboxymethyl transferase utilized for selective tRNA wobble modification.
Nucleic Acids Res., 43:4602-4613, 2015

PubMed Abstract: Enzyme-mediated modifications at the wobble position of tRNAs are essential for the translation of the genetic code. We report the genetic, biochemical and structural characterization of CmoB, the enzyme that recognizes the unique metabolite carboxy-S-adenosine-L-methionine (Cx-SAM) and catalyzes a carboxymethyl transfer reaction resulting in formation of 5-oxyacetyluridine at the wobble position of tRNAs. CmoB is distinctive in that it is the only known member of the SAM-dependent methyltransferase (SDMT) superfamily that utilizes a naturally occurring SAM analog as the alkyl donor to fulfill a biologically meaningful function. Biochemical and genetic studies define the in vitro and in vivo selectivity for Cx-SAM as alkyl donor over the vastly more abundant SAM. Complementary high-resolution structures of the apo- and Cx-SAM bound CmoB reveal the determinants responsible for this remarkable discrimination. Together, these studies provide mechanistic insight into the enzymatic and non-enzymatic feature of this alkyl transfer reaction which affords the broadened specificity required for tRNAs to recognize multiple synonymous codons.

PubMed: 25855808
DOI: 10.1093/nar/gkv206

実験手法

X-RAY DIFFRACTION (2.619 Å)