Guanylate kinase

spinqualitylabelsall models E. coli guanylate kinase complex with GMP, sulfate (PDB entry 2anb) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Guanylate kinase (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains. Structural highlights The biological assembly of E. coli guanylate kinase is homohexamer. The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain. 3D structures of guanylate kinase Guanylate kinase 3D structures

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