GMP synthase

spinqualitylabelsall models Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate (PDB entry 2vxo) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function GMP synthase (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate. GMPS is active in purine and glutamate metabolism. GMPS is a bifunctional two-domain enzyme with the N-terminal glutaminase dominates extracts ammonia from glutamine and the C-terminal synthetase adds amine group to XMP to produce GMP. Structural highlights Human GMPS structure contains 2 dimerization domains (D1 and D2). The active site is located between the synthetase domain and D2 domain and covered by the LID motif. The catalytic triad consists of Cys, His and Glu. 3D structures of GMP synthase Updated on 21-March-2016 1wl8, 2d7j – PhGMPS subunit A – Pyrococcus horikoshii 2dpl, 3a4i - PhGMPS subunit B 2ywb – TtGMPS – Thermus thermophilus 3tqi – GMPS – Coxiella burnetii 1kxj – TmGMPS – Thermotoga maritima 2a9v – GMPS – Thermoplasma acidophilum 2lxn – GMPS subunit A – Methanocaldococcus jannaschii 2vpi – hGMPS glutaminase domain – human 2vxo - hGMPS + XMP 2ywc – TtGMPS + XMP 2iss – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS 1gpm – GMPS + pyrophosphate + AMP – Escherichia coli

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