2A7R

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

2A7R の概要

• エントリーDOI: 10.2210/pdb2a7r/pdb
• 分子名称: GMP reductase 2, SULFATE ION, GUANOSINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 161476.41

構造登録者

Li, J.,Wei, Z.,Zheng, M.,Gu, X.,Deng, Y.,Qiu, R.,Chen, F.,Ji, C.,Gong, W.,Xie, Y.,Mao, Y. (登録日: 2005-07-05, 公開日: 2006-01-31, 最終更新日: 2024-12-25)

主引用文献

Li, J.,Wei, Z.,Zheng, M.,Gu, X.,Deng, Y.,Qiu, R.,Chen, F.,Ji, C.,Gong, W.,Xie, Y.,Mao, Y.
Crystal Structure of Human Guanosine Monophosphate Reductase 2 (GMPR2) in Complex with GMP
J.Mol.Biol., 355:980-988, 2006

PubMed Abstract: Guanosine monophosphate reductase (GMPR) catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP, and plays a critical role in re-utilization of free intracellular bases and purine nucleosides. Here, we report the first crystal structure of human GMP reductase 2 (hGMPR2) in complex with GMP at 3.0 A resolution. The protein forms a tetramer composed of subunits adopting the ubiquitous (alpha/beta)8 barrel fold. Interestingly, the substrate GMP is bound to hGMPR2 through interactions with Met269, Ser270, Arg286, Ser288, and Gly290; this makes the conformation of the adjacent flexible binding region (residues 268-289) fixed, much like a door on a hinge. Structure comparison and sequence alignment analyses show that the conformation of the active site loop (residues 179-187) is similar to those of hGMPR1 and inosine monophosphate dehydrogenases (IMPDHs). We propose that Cys186 is the potential active site, and that the conformation of the loop (residues 129-133) suggests a preference for the coenzyme NADPH over NADH. This structure provides important information towards understanding the functions of members of the GMPR family.

PubMed: 16359702
DOI: 10.1016/j.jmb.2005.11.047

実験手法

X-RAY DIFFRACTION (3 Å)