Guanylate kinase

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{{STRUCTURE_1gky| PDB=1gky | SIZE=400| SCENE= |right|CAPTION=Yeast guanylate kinase complex with GMP, sulfate and acetyl group [[1gky]] }}
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<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP, sulfate (PDB entry [[2anb]])' scene='48/487529/Cv/1'>
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== Function ==
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'''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.
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== Structural highlights ==
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The biological assembly of ''E. coli'' guanylate kinase is <scene name='48/487529/Cv/9'>homohexamer</scene>. The <scene name='48/487529/Cv/10'>GMP binding site</scene> of GK is <scene name='48/487529/Cv/8'>located between its nucleoside monophosphate-binding domain and the LID domain</scene><ref>PMID:16140325</ref>.
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to a Jmol applet. Check out the other buttons as well!
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'''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 to a GK domain. The GK domain has no catalytic activity. The MAGUK contain PDZ, WW, SH3 and GK domains.
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==3D structures of guanylate kinase==
==3D structures of guanylate kinase==
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[[Guanylate kinase 3D structures]]
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[[1ex6]] – yGK – yeast<br />
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</StructureSection>
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[[3sqk]] – yGK (mutant)<br />
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[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />
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[[1z8f]] – MtGK (mutant)<br />
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[[1s96]], [[2anc]] – EcGK – ''Escherichia coli''<br />
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[[1z6g]] – GK – ''Plasmodium falciparum''
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'''Guanylate kinase binary complex'''
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[[1gky]], [[1ex7]] – yGK + GMP <br />
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[[1lvg]] – GK + ADP + GMP – mouse<br />
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[[2an9]] – EcGK + guanosine + GDP<br />
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[[2anb]] – EcGK + GMP<br />
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[[2f3t]] – EcGK + GMP derivative<br />
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[[2f3r]] – EcGK + adenosyl-guanosyl pentaphosphate<br />
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[[1znx]] – MtGK + GMP<br />
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[[1zny]], [[1znz]] – MtGK + GDP<br />
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[[2j41]] – GK + GMP – ''Staphylococcus aureus''<br />
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[[2qor]] - GK + GMP – ''Plasmodium vivax''<br />
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[[3lnc]] - GK + GMP – ''Anaplasma phagocytophilum''<br />
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[[3tr0]] – GK residues 1-202 + GMP – ''Coxiella burnetii''
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'''Membrane-associated guanylate kinase'''
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[[1uep]] – hMAGUK PDZ domain 3 – human – NMR<BR />
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[[1ueq]], [[2kpk]] - hMAGUK PDZ domain 1 – NMR<BR />
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[[1ujv]] - hMAGUK PDZ domain 2 – NMR<BR />
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[[3bpu]] - hMAGUK PDZ domain 3 (mutant)<br />
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[[3soe]] - hMAGUK PDZ domain 3<br />
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[[2q9v]] - hMAGUK PDZ domain 4<br />
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[[1uew]] - hMAGUK PDZ domain 4 – NMR<BR />
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[[1wfv]] - hMAGUK PDZ domain 5 – NMR<BR />
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[[2r4h]] - hMAGUK PDZ domain 6 (mutant)<br />
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[[2i04]] - hMAGUK PDZ domain 1 + papillomavirus peptide<br />
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[[2kpl]] - hMAGUK PDZ domain 1 + protein E6 peptide]] - NMR<BR />
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[[2ysd]], [[2yse]] - hMAGUK WW domain – NMR<BR />
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[[2zaj]] - hMAGUK WW 2 domain – NMR<BR />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

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References

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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