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. Whole active site. N-terminal glutaminase domain contains catalytic triad Cys104, His190, Glu192. 3D structures of GMP synthase Updated on 04-June-2017 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 5tw7 – GMPS – Neisseria gonorrhoeae

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