2J2C

Crystal structure of Human Cytosolic 5'-Nucleotidase II (NT5C2, cN-II)

2J2C の概要

• エントリーDOI: 10.2210/pdb2j2c/pdb
• 分子名称: CYTOSOLIC PURINE 5'-NUCLEOTIDASE, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: cytosolic 5-prime nucleotidase ii, allosteric enzyme, gmp- imp specific nucleotidase, high km 5-prime nucleotidase, cn- ii, nt5c2, hydrolase, cytosolic purine 5- prime nucleotidase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64781.71

構造登録者

Wallden, K.,Stenmark, P.,Arrowsmith, C.,Berglund, H.,Busam, R.,Collins, R.,Edwards, A.,Ehn, M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Hallberg, B.M.,Holmberg Schiavone, L.,Hogbom, M.,Karlberg, T.,Kotenyova, T.,Loppnau, P.,Magnusdottir, A.,Nilsson-Ehle, P.,Nyman, T.,Ogg, D.,Persson, C.,Sagemark, J.,Sundstrom, M.,Uppenberg, J.,Thorsell, A.G.,Van Den Berg, S.,Weigelt, J.,Welin, M.,Nordlund, P. (登録日: 2006-08-16, 公開日: 2006-09-19, 最終更新日: 2023-12-13)

主引用文献

Wallden, K.,Stenmark, P.,Nyman, T.,Flodin, S.,Graslund, S.,Loppnau, P.,Bianchi, V.,Nordlund, P.
Crystal Structure of Human Cytosolic 5'- Nucleotidase II: Insights Into Allosteric Regulation and Substrate Recognition
J.Biol.Chem., 282:17828-, 2007

PubMed Abstract: Cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates and regulates the IMP and GMP pools within the cell. It possesses phosphotransferase activity and thereby also catalyzes the reverse reaction. Both reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. We have solved structures of cytosolic 5'-nucleotidase II as native protein (2.2 Angstrom) and in complex with adenosine (1.5 Angstrom) and beryllium trifluoride (2.15 Angstrom) The tetrameric enzyme is structurally similar to enzymes of the haloacid dehalogenase (HAD) superfamily, including mitochondrial 5'(3')-deoxyribonucleotidase and cytosolic 5'-nucleotidase III but possesses additional regulatory regions that contain two allosteric effector sites. At effector site 1 located near a subunit interface we modeled diadenosine tetraphosphate with one adenosine moiety in each subunit. This efficiently glues the tetramer subunits together in pairs. The model shows why diadenosine tetraphosphate but not diadenosine triphosphate activates the enzyme and supports a role for cN-II during apoptosis when the level of diadenosine tetraphosphate increases. We have also modeled 2,3-bisphosphoglycerate in effector site 1 using one phosphate site from each subunit. By comparing the structure of cytosolic 5'-nucleotidase II with that of mitochondrial 5'(3')-deoxyribonucleotidase in complex with dGMP, we identified residues involved in substrate recognition.

PubMed: 17405878
DOI: 10.1074/JBC.M700917200

実験手法

X-RAY DIFFRACTION (2.2 Å)