1WNG

Structural study of project ID PH0725 from Pyrococcus horikoshii OT3

1WNG の概要

• エントリーDOI: 10.2210/pdb1wng/pdb
• 分子名称: Probable diphthine synthase, SULFATE ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: transferase, methyltransferase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60187.52

構造登録者

Kunishima, N.,Shimizu, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-08-02, 公開日: 2005-07-19, 最終更新日: 2024-03-13)

主引用文献

Kishishita, S.,Shimizu, K.,Murayama, K.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Kunishima, N.
Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2.
Acta Crystallogr.,Sect.D, 64:397-406, 2008

PubMed Abstract: The target of diphtheria toxin is the diphthamide residue in translation elongation factor 2 (EF-2), which is generated by a three-step post-translational modification of a specific histidine residue in the EF-2 precursor. In the second modification step, an S-adenosylmethionine-dependent methyltransferase, diphthine synthase (DS), catalyzes the trimethylation of the EF-2 precursor. The homodimeric crystal structures of the archaeal diphthine synthases from Pyrococcus horikoshii OT3 and Aeropyrum pernix K1 have been determined. These structures share essentially the same overall fold as the cobalt-precorrin-4 methyltransferase CbiF, confirming that DS belongs to the dimeric class III family of methyltransferases. In the P. horikoshii DS dimer, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine (AdoHcy), while the other active site contains no ligand. This asymmetric AdoHcy binding may be a consequence of intra-domain and inter-domain movements upon binding of AdoHcy at one of the two sites. These movements disrupt the twofold dimeric symmetry of the DS dimer and probably cause lower AdoHcy affinity at the other binding site.

PubMed: 18391406
DOI: 10.1107/S0907444908000723

実験手法

X-RAY DIFFRACTION (2.1 Å)