5NM8

Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942, with PLP bound

5NM8 の概要

• エントリーDOI: 10.2210/pdb5nm8/pdb
• 関連するPDBエントリー: 5NLC
• 分子名称: PipY, PYRIDOXAL-5'-PHOSPHATE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: fold type iii plp-protein, vitamin b6, pyridoxal phosphate, schiff base, plp-binding protein
• 由来する生物種: Synechococcus elongatus (strain PCC 7942)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51134.19

構造登録者

Tremino, L.,Forcada-Nadal, A.,Contreras, A.,Rubio, V. (登録日: 2017-04-05, 公開日: 2017-09-13, 最終更新日: 2024-01-17)

主引用文献

Tremino, L.,Forcada-Nadal, A.,Contreras, A.,Rubio, V.
Studies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B6 -dependent epilepsy.
FEBS Lett., 591:3431-3442, 2017

PubMed Abstract: The Synechococcus elongatus COG0325 gene pipY functionally interacts with the nitrogen regulatory gene pipX. As a first step toward a molecular understanding of such interactions, we characterized PipY. This 221-residue protein is monomeric and hosts pyridoxal phosphate (PLP), binding it with limited affinity and losing it upon incubation with D-cycloserine. PipY crystal structures with and without PLP reveal a single-domain monomer folded as the TIM barrel of type-III fold PLP enzymes, with PLP highly exposed, fitting a role for PipY in PLP homeostasis. The mobile PLP phosphate-anchoring C-terminal helix might act as a trigger for PLP exchange. Exploiting the universality of COG0325 functions, we used PipY in site-directed mutagenesis studies to shed light on disease causation by epilepsy-associated mutations in the human COG0325 gene PROSC.

PubMed: 28914444
DOI: 10.1002/1873-3468.12841

実験手法

X-RAY DIFFRACTION (1.93 Å)