Structure of active conformations of UMP kinase from Dictyostelium discoideum 
suggest phosphoryl transfer is associative

Schlichting, Ilme; Reinstein, Jochen

doi:10.1021/bi970974c

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

Structure of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative

MPS-Authors

/persons/resource/persons95189

Schlichting, Ilme
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94928

Reinstein, Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://pubs.acs.org/doi/pdf/10.1021/bi970974c
(全文テキスト（全般）)

https://doi.org/10.1021/bi970974c
(全文テキスト（全般）)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Schlichting, I., & Reinstein, J. (1997). Structure of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry, 36, 9290-9296. doi:10.1021/bi970974c.

引用: https://hdl.handle.net/11858/00-001M-0000-0019-A65E-C

要旨

UMP/CMP kinase from Dictyostelium discoideum (UmpKdicty) catalyzes the specific transfer of the terminal phosphate of ATP to UMP or CMP. Crystal structures of UmpKdicty with substrates and the transition state analogs AlF3 or BeF2 that lock UmpKdicty in active conformations were solved. The positions of the catalytic Mg2+ and the highly conserved lysine of the P loop are virtually invariant in the different structures. In contrast, catalytic arginines move to stabilize charges that develop during this reaction. The location of the arginines indicates formation of negative charges during the reaction at the transferred phosphoryl group, but not at the phosphate bridging oxygen atoms. This is consistent with an associative phosphoryl transfer mechanism but not with a dissociative one.