2VBU

Riboflavin kinase Mj0056 from Methanocaldococcus jannaschii in complex with CDP

2VBU の概要

• エントリーDOI: 10.2210/pdb2vbu/pdb
• 関連するPDBエントリー: 2P3M 2VBS 2VBT 2VBV
• 分子名称: RIBOFLAVIN KINASE, CYTIDINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase, cradle-loop barrel, ctp-dependent kinase, fmn
• 由来する生物種: METHANOCOCCUS JANNASCHII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16491.52

構造登録者

Hartmann, M.D.,Ammelburg, M.,Djuranovic, S.,Martin, J.,Lupas, A.N.,Zeth, K. (登録日: 2007-09-16, 公開日: 2007-11-20, 最終更新日: 2023-12-13)

主引用文献

Ammelburg, M.,Hartmann, M.D.,Djuranovic, S.,Alva, V.,Koretke, K.K.,Martin, J.,Sauer, G.,Truffault, V.,Zeth, K.,Lupas, A.N.,Coles, M.
A Ctp-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels.
Structure, 15:1577-, 2007

PubMed Abstract: Proteins of the cradle-loop barrel metafold are formed by duplication of a conserved betaalphabeta-element, suggesting a common evolutionary origin from an ancestral group of nucleic acid-binding proteins. The basal fold within this metafold, the RIFT barrel, is also found in a wide range of enzymes, whose homologous relationship with the nucleic acid-binding group is unclear. We have characterized a protein family that is intermediate in sequence and structure between the basal group of cradle-loop barrels and one family of RIFT-barrel enzymes, the riboflavin kinases. We report the structure, substrate-binding mode, and catalytic activity for one of these proteins, Methanocaldococcus jannaschii Mj0056, which is an archaeal riboflavin kinase. Mj0056 is unusual in utilizing CTP rather than ATP as the donor nucleotide, and sequence conservation in the relevant residues suggests that this is a general feature of archaeal riboflavin kinases.

PubMed: 18073108
DOI: 10.1016/J.STR.2007.09.027

実験手法

X-RAY DIFFRACTION (1.7 Å)