Guanylate kinase
From Proteopedia
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<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry [[2anb]])' scene=''> | <StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry [[2anb]])' scene=''> | ||
== Function == | == 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 | + | '''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<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 == | == Structural highlights == | ||
The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>. | The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>. | ||
| - | + | </StructureSection> | |
==3D structures of guanylate kinase== | ==3D structures of guanylate kinase== | ||
Revision as of 07:25, 20 March 2016
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3D structures of guanylate kinase
Updated on 20-March-2016
References
- ↑ Johnston CA, Whitney DS, Volkman BF, Doe CQ, Prehoda KE. Conversion of the enzyme guanylate kinase into a mitotic-spindle orienting protein by a single mutation that inhibits GMP-induced closing. Proc Natl Acad Sci U S A. 2011 Nov 1;108(44):E973-8. Epub 2011 Oct 11. PMID:21990344 doi:10.1073/pnas.1104365108
- ↑ Hible G, Renault L, Schaeffer F, Christova P, Zoe Radulescu A, Evrin C, Gilles AM, Cherfils J. Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase. J Mol Biol. 2005 Oct 7;352(5):1044-59. PMID:16140325 doi:10.1016/j.jmb.2005.07.042
