2IEW

Crystal structure of Inositol Phosphate Multikinase Ipk2 from S. cerevisiae

2IEW の概要

• エントリーDOI: 10.2210/pdb2iew/pdb
• 分子名称: Inositol polyphosphate multikinase, CALCIUM ION (3 entities in total)
• 機能のキーワード: atp-grasp fold related, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P07250
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82986.19

構造登録者

Holmes, W.,Jogl, G. (登録日: 2006-09-19, 公開日: 2006-10-24, 最終更新日: 2024-02-21)

主引用文献

Holmes, W.,Jogl, G.
Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity.
J.Biol.Chem., 281:38109-38116, 2006

PubMed Abstract: Inositol polyphosphates perform essential functions as second messengers in eukaryotic cells, and their cellular levels are regulated by inositol phosphate kinases. Most of these enzymes belong to the inositol phosphate kinase superfamily, which consists of three subgroups, inositol 3-kinases, inositol phosphate multikinases, and inositol hexakisphosphate kinases. Family members share several strictly conserved signature motifs and are expected to have the same backbone fold, despite very limited overall amino acid sequence identity. Sequence differences are expected to play important roles in defining the different substrate selectivity of these enzymes. To investigate the structural basis for substrate specificity, we have determined the crystal structure of the yeast inositol phosphate multikinase Ipk2 in the apoform and in a complex with ADP and Mn(2+) at up to 2.0A resolution. The overall structure of Ipk2 is related to inositol trisphosphate 3-kinase. The ATP binding site is similar in both enzymes; however, the inositol binding domain is significantly smaller in Ipk2. Replacement of critical side chains in the inositolbinding site suggests how modification of substrate recognition motifs determines enzymatic substrate preference and catalysis.

PubMed: 17050532
DOI: 10.1074/jbc.M606883200

実験手法

X-RAY DIFFRACTION (2 Å)