4ADT

Crystal structure of plasmodial PLP synthase

4ADT の概要

• エントリーDOI: 10.2210/pdb4adt/pdb
• 関連するPDBエントリー: 4ADS 4ADU
• 分子名称: PYRIDOXINE BIOSYNTHETIC ENZYME PDX1 HOMOLOGUE, PUTATIVE, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: transferase, pyridoxal 5-phosphate biosynthesis
• 由来する生物種: PLASMODIUM BERGHEI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65845.90

構造登録者

Guedez, G.,Sinning, I.,Tews, I. (登録日: 2012-01-03, 公開日: 2012-01-25, 最終更新日: 2023-12-20)

主引用文献

Guedez, G.,Hipp, K.,Windeisen, V.,Derrer, B.,Gengenbacher, M.,Boettcher, B.,Sinning, I.,Kappes, B.,Tews, I.
Assembly of the Eukaryotic Plp-Synthase Complex from Plasmodium and Activation of the Pdx1 Enzyme.
Structure, 20:172-, 2012

PubMed Abstract: Biosynthesis of vitamins is fundamental to malaria parasites. Plasmodia synthesize the active form of vitamin B(6) (pyridoxal 5'-phosphate, PLP) using a PLP synthase complex. The EM analysis shown here reveals a random association pattern of up to 12 Pdx2 glutaminase subunits to the dodecameric Pdx1 core complex. Interestingly, Plasmodium falciparum PLP synthase organizes in fibers. The crystal structure shows differences in complex formation to bacterial orthologs as interface variations. Alternative positioning of an α helix distinguishes an open conformation from a closed state when the enzyme binds substrate. The pentose substrate is covalently attached through its C1 and forms a Schiff base with Lys84. Ammonia transfer between Pdx2 glutaminase and Pdx1 active sites is regulated by a transient tunnel. The mutagenesis analysis allows defining the requirement for conservation of critical methionines, whereas there is also plasticity in ammonia tunnel construction as seen from comparison across different species.

PubMed: 22244765
DOI: 10.1016/J.STR.2011.11.015

実験手法

X-RAY DIFFRACTION (2.42 Å)