4LYG

Crystal structure of human PRS1 E43T mutant

4LYG の概要

• エントリーDOI: 10.2210/pdb4lyg/pdb
• 関連するPDBエントリー: 3S5J 4LZN 4LZO 4M0P 4M0U
• 分子名称: Ribose-phosphate pyrophosphokinase 1, SULFATE ION (2 entities in total)
• 機能のキーワード: prs1, atp r5p, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72325.04

構造登録者

Chen, P.,Teng, M.,Li, X. (登録日: 2013-07-31, 公開日: 2015-02-04, 最終更新日: 2024-03-20)

主引用文献

Chen, P.,Liu, Z.,Wang, X.,Peng, J.,Sun, Q.,Li, J.,Wang, M.,Niu, L.,Zhang, Z.,Cai, G.,Teng, M.,Li, X.
Crystal and EM Structures of Human Phosphoribosyl Pyrophosphate Synthase I (PRS1) Provide Novel Insights into the Disease-Associated Mutations
Plos One, 10:e0120304-e0120304, 2015

PubMed Abstract: Human PRS1, which is indispensable for the biosynthesis of nucleotides, deoxynucleotides and their derivatives, is associated directly with multiple human diseases because of single base mutation. However, a molecular understanding of the effect of these mutations is hampered by the lack of understanding of its catalytic mechanism. Here, we reconstruct the 3D EM structure of the PRS1 apo state. Together with the native stain EM structures of AMPNPP, AMPNPP and R5P, ADP and the apo states with distinct conformations, we suggest the hexamer is the enzymatically active form. Based on crystal structures, sequence analysis, mutagenesis, enzyme kinetics assays, and MD simulations, we reveal the conserved substrates binding motifs and make further analysis of all pathogenic mutants.

PubMed: 25781187
DOI: 10.1371/journal.pone.0120304

実験手法

X-RAY DIFFRACTION (3 Å)