4L0W

Plasmodium yoelii Prx1a modified at the N-terminus forms an artifactual octamer

4L0W の概要

• エントリーDOI: 10.2210/pdb4l0w/pdb
• 関連するPDBエントリー: 4L0U
• 分子名称: Thioredoxin peroxidase 1, ACETATE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, peroxiredoxin, disulfide, antioxidant
• 由来する生物種: Plasmodium yoelii yoelii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23422.51

構造登録者

Gretes, M.C.,Karplus, P.A. (登録日: 2013-06-01, 公開日: 2016-11-09, 最終更新日: 2023-09-20)

主引用文献

Gretes, M.C.,Karplus, P.A.
Observed octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag.
Protein Sci., 22:1445-1452, 2013

PubMed Abstract: Peroxiredoxins (Prxs) are ubiquitous and efficient antioxidant enzymes crucial for redox homeostasis in most organisms, and are of special importance for disease-causing parasites that must protect themselves against the oxidative weapons of the human immune system. Here, we describe reanalyses of crystal structures of two Prxs from malaria parasites. In addition to producing improved structures, we provide normalizing explanations for features that had been noted as unusual in the original report of these structures (Qiu et al., BMC Struct Biol 2012;12:2). Most importantly, we provide evidence that the unusual octameric assembly seen for Plasmodium yoelii Prx1a is not physiologically relevant, but arises because the structure is not of authentic P. yoelii Prx1a, but a variant we designate PyPrx1a(N*) that has seven native N-terminal residues replaced by an affinity tag. This N-terminal modification disrupts a previously unrecognized, hydrophobic "ball-and-socket" interaction conserved at the B-type dimer interface of Prx1 subfamily enzymes, and is accommodated by a fascinating two-residue "β-slip" type register shift in the β-strand association at a dimer interface. The resulting change in the geometry of the dimer provides a simple explanation for octamer formation. This study illustrates how substantive impacts can occur in protein variants in which native residues have been altered.

PubMed: 23934758
DOI: 10.1002/pro.2328

実験手法

X-RAY DIFFRACTION (2.29 Å)