Guanylate kinase: Difference between revisions

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</StructureSection>
</StructureSection>
==3D structures of guanylate kinase==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Guanylate kinase
**[[6nui]] - hGK - human<br />
**[[1ex6]], [[4f4j]] – yGK – yeast<br />
**[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />
**[[1z8f]] – MtGK (mutant)<br />
**[[1s96]], [[2anc]] – EcGK – ''Escherichia coli''<br />
**[[1z6g]] – GK – ''Plasmodium falciparum''
*Guanylate kinase complex
**[[1lvg]] – mGK + ADP + GMP – mouse<br />
**[[1gky]], [[1ex7]] – yGK + GMP <br />
**[[2an9]] – EcGK + guanosine + GDP<br />
**[[2anb]] – EcGK + GMP<br />
**[[2f3t]] – EcGK + GMP derivative<br />
**[[2f3r]] – EcGK + adenosyl-guanosyl pentaphosphate<br />
**[[1znx]] – MtGK + GMP<br />
**[[1zny]], [[1znz]] – MtGK + GDP<br />
**[[2j41]] – SaGK + GMP – ''Staphylococcus aureus''<br />
**[[4qrh]] - SaGK + (P)PPGPP<br />
**[[2qor]] - GK + GMP – ''Plasmodium vivax''<br />
**[[3lnc]] - GK + GMP – ''Anaplasma phagocytophilum''<br />
**[[3tr0]] – GK residues 1-202 + GMP – ''Coxiella burnetii''<br />
**[[6mfu]] - GK + GMP + ADP – ''Cryprococcus neoformans''<br />
*Membrane-associated guanylate kinase WW and PDZ domain-containing protein 1; Domains – WW 295-388; PDZ1 455-580; PDZ3 640-721; PDZ4 839-922; PDZ6 1149-1233
**[[2kpk]] – hMAGI-1 PDZ1 – NMR<br />
**[[3bpu]] – hMAGI-1 PDZ3 (mutant) <br />
**[[2q9v]] - hMAGI-1 PDZ4 (mutant) <br />
**[[2r4h]] – hMAGI-1 PDZ6 (mutant) <br />
**[[2i04]] – hMAGI-1 PDZ1 + papillomavirus peptide<br />
**[[5n7d]], [[5n7f]], [[5n7g]] - hMAGI-1 PDZ1 + RSK1 peptide<br />
**[[2kpl]] – hMAGI-1 PDZ1 + protein E6 peptide - NMR<br />
**[[2ysd]], [[2yse]] – hMAGI-1 WW domain – NMR<br />
**[[2zaj]] – hMAGI-1 WW domain – NMR<br />
**[[5zys]] – mMAGI-1 PDZ4 + nephrin<br />
*Membrane-associated guanylate kinase inverted-2; Domains – PDZ1 454-564; PDZ2 642-724; PDZ3 802-981; PDZ4 943-1043; PDZ5 1169-1258
**[[1ueq]] – hMAGI-2 PDZ1 – NMR<br />
**[[1ujv]] – hMAGI-2 PDZ2 – NMR<br />
**[[1uep]] – hMAGI-2 PDZ3 – NMR<br />
**[[1uew]] – hMAGI-2 PDZ4 – NMR<br />
**[[1wfv]] – hMAGI-2 PDZ5 – NMR<br />
*Membrane-associated guanylate kinase WW and PDZ domain-containing protein 3
**[[3soe]] – hMAGI-3 PDZ3 residues 601-691<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:17, 21 July 2019

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[1]. 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 . The of GK is [2].

3D structures of guanylate kinase

Guanylate kinase 3D structures


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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

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Michal Harel, Alexander Berchansky
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