3UKD

UMP/CMP KINASE FROM SLIME MOLD COMPLEXED WITH ADP, CMP, AND ALF3

3UKD の概要

• エントリーDOI: 10.2210/pdb3ukd/pdb
• 分子名称: URIDYLMONOPHOSPHATE/CYTIDYLMONOPHOSPHATE KINASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: nucleoside monophosphate kinase, nmp kinase, phosphoryl transfer, transition state analog complex, transferase
• 由来する生物種: Dictyostelium discoideum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22829.53

構造登録者

Schlichting, I.,Reinstein, J. (登録日: 1997-05-20, 公開日: 1998-05-20, 最終更新日: 2024-02-28)

主引用文献

Schlichting, I.,Reinstein, J.
Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative.
Biochemistry, 36:9290-9296, 1997

PubMed Abstract: 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.

PubMed: 9280438
DOI: 10.1021/bi970974c

実験手法

X-RAY DIFFRACTION (1.9 Å)