2a7r

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spinqualitylabelsall models 2a7r, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

Overview

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.

About this Structure

2A7R is a Single protein structure of sequence from Homo sapiens with SO4 and 5GP as ligands. Active as GMP reductase, with EC number 1.7.1.7 Full crystallographic information is available from OCA.

Reference

Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP., Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y, J Mol Biol. 2006 Feb 3;355(5):980-8. Epub 2005 Dec 1. PMID:16359702

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