GTP-binding protein

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'''GTP-binding proteins''' or '''G proteins''' are transmitting signals outside the cell which cause changes within the cell. They act as molecular switches which are on when binding GTP and off when binding GDP. GTP-binding proteins belong to two families: '''heterotrimeric G proteins'''<ref>PMID:14762218</ref> see [[Transducin]] and '''small GTPases'''<ref>PMID:11152757</ref>. The structure of small GTPase is homologous to that of the α subunit of heterotrimeric G protein. See details on '''small GTP-binding protein LepA''' in [[LepA]].
'''GTP-binding proteins''' or '''G proteins''' are transmitting signals outside the cell which cause changes within the cell. They act as molecular switches which are on when binding GTP and off when binding GDP. GTP-binding proteins belong to two families: '''heterotrimeric G proteins'''<ref>PMID:14762218</ref> see [[Transducin]] and '''small GTPases'''<ref>PMID:11152757</ref>. The structure of small GTPase is homologous to that of the α subunit of heterotrimeric G protein. See details on '''small GTP-binding protein LepA''' in [[LepA]].
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'''Heterotrimeric G protein or guanine nucleotide-binding protein or G protein''' (GNBP) are heterodimeric membrane proteins composed of α, β and γ subunits. GNBP is involved in mammalian cellular signaling pathways. GNBP α subunit binds GDP or GTP. When bound to GTP it dissociates from the β and γ subunits, binds to adenylate cyclase which converts ATP to cAMP. See also<br />
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'''Heterotrimeric G protein or guanine nucleotide-binding protein or G protein''' (GNBP) are heterodimeric membrane proteins composed of α, β and γ subunits. GNBP is involved in mammalian cellular signaling pathways. GNBP α subunit binds GDP or GTP. When bound to GTP it dissociates from the β and γ subunits, binds to adenylate cyclase which converts ATP to cAMP. See also<br />
[[G protein-coupled receptor]]<br />
[[G protein-coupled receptor]]<br />
[[Beta2 adrenergic receptor-Gs protein complex]].
[[Beta2 adrenergic receptor-Gs protein complex]].
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== Structural highlights ==
== Structural highlights ==
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''E. coli'' small GTPase ERA binds GDP in a cavity formed by <scene name='46/463251/Cv/9'>7 highly conserved regions G1, G4, G5</scene><ref>PMID:19706445</ref>. <scene name='46/463251/Cv/8'>GDP binding site</scene>. Water molecules are shown as red spheres.
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''E. coli'' <scene name='46/463251/Cv/11'>small GTPase ERA binds GDP in a cavity</scene> formed by <scene name='46/463251/Cv/9'>7 highly conserved regions G1, G4, G5</scene><ref>PMID:19706445</ref>. <scene name='46/463251/Cv/8'>GDP binding site</scene>. Water molecules are shown as red spheres.
== 3D Structures of GTP-binding protein ==
== 3D Structures of GTP-binding protein ==

Revision as of 13:11, 27 October 2019

E. coli small GTP-binding protein ERA complex with GDP and sulfate (PDB code 3ieu)

Drag the structure with the mouse to rotate


See Also

References

  1. ↑ Preininger AM, Hamm HE. G protein signaling: insights from new structures. Sci STKE. 2004 Jan 27;2004(218):re3. PMID:14762218 doi:http://dx.doi.org/10.1126/stke.2182004re3
  2. ↑ Takai Y, Sasaki T, Matozaki T. Small GTP-binding proteins. Physiol Rev. 2001 Jan;81(1):153-208. PMID:11152757
  3. ↑ Lania A, Mantovani G, Spada A. G protein mutations in endocrine diseases. Eur J Endocrinol. 2001 Nov;145(5):543-59. PMID:11720871
  4. ↑ Moreno-Velasquez SD, Seidel C, Juvvadi PR, Steinbach WJ, Read ND. Caspofungin-Mediated Growth Inhibition and Paradoxical Growth in Aspergillus fumigatus Involve Fungicidal Hyphal Tip Lysis Coupled with Regenerative Intrahyphal Growth and Dynamic Changes in beta-1,3-Glucan Synthase Localization. Antimicrob Agents Chemother. 2017 Sep 22;61(10). pii: AAC.00710-17. doi:, 10.1128/AAC.00710-17. Print 2017 Oct. PMID:28760907 doi:http://dx.doi.org/10.1128/AAC.00710-17
  5. ↑ Tu C, Zhou X, Tropea JE, Austin BP, Waugh DS, Court DL, Ji X. Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis. Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14843-8. Epub 2009 Aug 17. PMID:19706445
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