Guanylate kinase

(Difference between revisions)

Revision as of 07:16, 20 March 2016

E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry 2anb)

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-{{STRUCTURE_1gky|  PDB=1gky  | SIZE=400| SCENE= |right|CAPTION=Yeast guanylate kinase complex with GMP (stick model), sulfate and acetyl group [[1gky]] }}
+<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry [[2anb]])' scene=''>
+== 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<ref>PMID:8528769</ref>.  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<ref>PMID:21990344</ref>.  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 GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>.
 ==3D structures of guanylate kinase==