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Receiver domain of sensor histidine kinase CKI1: Difference between revisions

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<StructureSection load='3mmn' size='400' side='right' caption='Magnesium-bound form of CKI1RD, (PDB entry [[3mmn]])' scene='Receiver_domain/Initial_1/2'>
[[Image:Receiver_domain_surf.png|250px|left|thumb| Receiver domain of CKI1 from ''Arabidopsis'', [[3mmn]]]]
[[Image:Receiver_domain_surf.png|250px|left|thumb| Receiver domain of CKI1 from ''Arabidopsis'', [[3mmn]]]]


{{STRUCTURE_3mmn| right| PDB=3mmn |
[[3mmn]] }}


'''Receiver domain of sensor histidine kinase CKI1''' (CKI1RD) catalyses the transphosphorylation reaction during hormonal and abiotic signalling in plants. Membrane-bound histidine kinase Cytokinin-independet 1 '''(CKI1)''' is a member of the Multistep phosphorelay '''(MSP)''' signalling pathway in ''Arabidopsis''. CKI1 was found to be constitutively active activator of a cytokinin-like response. Intracellularly located C-terminal CKI1RD is responsible for the recognition of CKI1 downstream signalling partners from family of Arabidopsis histidine-containing phosphotransfer proteins '''(AHP)''' and triggers the cytokinin-like signal transmission. Divalent magnesium ion bound in the active site of CKI1RD is essential for the transphosphorylation reaction. Crystal structure of CKI1RD was determined as magnesium free and magnesium bound form. Magnesium binding induces the rearrangement of residues around the active site of CKI1RD, as was determined by both X-ray crystallography and NMR spectroscopy.




'''Receiver domain of sensor histidine kinase CKI1''' (CKI1RD) catalyses the transphosphorylation reaction during hormonal and abiotic signalling in plants. Membrane-bound histidine kinase Cytokinin-independet 1 '''(CKI1)''' is a member of the Multistep phosphorelay '''(MSP)''' signalling pathway in ''Arabidopsis''. CKI1 was found to be constitutively active activator of a cytokinin-like response. Intracellularly located C-terminal CKI1RD is responsible for the recognition of CKI1 downstream signalling partners from family of Arabidopsis histidine-containing phosphotransfer proteins '''(AHP)''' and triggers the cytokinin-like signal transmission. Divalent magnesium ion bound in the active site of CKI1RD is essential for the transphosphorylation reaction. Crystal structure of CKI1RD was determined as magnesium-free and magnesium-bound form. Magnesium binding induces the rearrangement of residues around the active site of CKI1RD, as was determined by both X-ray crystallography and NMR spectroscopy.


== Biological Function ==
== Biological Function ==
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Recently was shown that CKI1RD is responsible for a specific interaction with individual subset of second messengers from AHP family (AHP2, AHP3, AHP5)<ref>PMID:21569135</ref>.
Recently was shown that CKI1RD is responsible for a specific interaction with individual subset of second messengers from AHP family (AHP2, AHP3, AHP5)<ref>PMID:21569135</ref>.


 
==CKI1RD structure and effects of magnesium binding in the active site==
 
==CKI1RD tructure and effects of magnesium binding in the active site==
<StructureSection load='3mmn' size='400' side='right' caption='CKI1RD magnesium-bound form, (PDB entry [[3mmn]])' scene='Receiver_domain/Initial_1/2'>
The crystal structure of CKI1RD shows the conformational conservation of RDs belonging to CheY-like protein superfamily <ref>PMID:8257674</ref><ref>PMID:19036790</ref>. CKI1RD is folded in a (α/β)5 manner with central β-sheet formed from parallel beta-strands (β2-β1-β3-β4-β5) surrounded on both sides by two (α1 and α5) and three (α2, α3, α4) α-helices. Secondary structure elements are connected by five loops L1-L5 on the face side of the protein. The active site with <scene name='Receiver_domain/Initial_1/6'> phosphoacceptor D1050</scene> is located at the C-termini of the central β3-strand in a pocket delineated loops L1, L3 and L5. A highly conserved <scene name='Receiver_domain/Initial_1/4'> triad of carboxyl oxygens</scene>, formed by D1050 together with D992 and D993 and carbonyl oxygen of <scene name='Receiver_domain/Initial_1/8'> Q1052</scene> give the active site an acidic character. This architecture of the active site is well conserved among CheY-like superfamily and corresponds to the phosphotransfer function of the receiver domains.
The crystal structure of CKI1RD shows the conformational conservation of RDs belonging to CheY-like protein superfamily <ref>PMID:8257674</ref><ref>PMID:19036790</ref>. CKI1RD is folded in a (α/β)5 manner with central β-sheet formed from parallel beta-strands (β2-β1-β3-β4-β5) surrounded on both sides by two (α1 and α5) and three (α2, α3, α4) α-helices. Secondary structure elements are connected by five loops L1-L5 on the face side of the protein. The active site with <scene name='Receiver_domain/Initial_1/6'> phosphoacceptor D1050</scene> is located at the C-termini of the central β3-strand in a pocket delineated loops L1, L3 and L5. A highly conserved <scene name='Receiver_domain/Initial_1/4'> triad of carboxyl oxygens</scene>, formed by D1050 together with D992 and D993 and carbonyl oxygen of <scene name='Receiver_domain/Initial_1/8'> Q1052</scene> give the active site an acidic character. This architecture of the active site is well conserved among CheY-like superfamily and corresponds to the phosphotransfer function of the receiver domains.
[[Image:Structural and sequentional conservation among receiver domains.png.PNG|250px|left|thumb| Conservation of the structure and sequence among known receiver domains. Left: Superimposition of 35 known crystal structures of receiver domains. Right: Representation of highly conserved residues among receiver domains.]]
[[Image:Structural and sequentional conservation among receiver domains.png.PNG|250px|left|thumb| Structure and sequence conservation among known receiver domains. Left: Superimposition of 35 known crystal structures of receiver domains. Right: Representation of highly conserved residues among receiver domains (CKI1RD numbering)]]
<scene name='Receiver_domain/Initial_1/2'>-restore original scene-</scene><br />
<scene name='Receiver_domain/Initial_1/2'>-restore original scene-</scene><br />
The octahedral coordination geometry of magnesium ion in this crystal is not complete. <scene name='Receiver_domain/Initial_1/9'> Magnesium ion</scene> is four-coordinated with carboxyl oxygens of D993 and D1050, carbonyl oxygen of Q1052 and with one water molecule that forms a hydrogen bridge to the carboxyl oxygen of D992.<br />
The octahedral coordination geometry of magnesium ion in this crystal is not complete. <scene name='Receiver_domain/Initial_1/9'> Magnesium ion</scene> is four-coordinated with carboxyl oxygens of D993 and D1050, carbonyl oxygen of Q1052 and with one water molecule that forms a hydrogen bridge to the carboxyl oxygen of D992.<br />
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</StructureSection>
</StructureSection>


== 3D Structures of CKI1RD ==
== 3D Structures of CKI1RD and similar receiver domains ==


[[3mm4]] - CKI1RD in metal free form<br />
[[3mm4]] - CKI1RD in metal free form<br />
[[3mmn]] - CKI1RD in magnesium bound form<br />
[[3mmn]] - CKI1RD in magnesium bound form<br />
[[3dcf]] - ETR1RD, receiver domain of plant hormone ethylene receptor from ''Arabidopsis''<br />
[[2chy]] - CheY, chemotaxis response regulatory protein from ''Salmonella enterica''<br />
[[3dgf]] - response regulatory signalling protein from ''Thermotoga maritina''<br />


== References ==
== References ==
<references />
<references />
[[Category:Topic Page]]
[[Category:Phosphotransferase]]

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