2A7R
Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)
Summary for 2A7R
| Entry DOI | 10.2210/pdb2a7r/pdb |
| Descriptor | GMP reductase 2, SULFATE ION, GUANOSINE-5'-MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 161476.41 |
| Authors | |
| Primary citation | 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 Cited by 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: 16359702DOI: 10.1016/j.jmb.2005.11.047 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
