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| | ==1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis== | | ==1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis== |
| - | <StructureSection load='2kwa' size='340' side='right' caption='[[2kwa]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kwa' size='340' side='right'caption='[[2kwa]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kwa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KWA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kwa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KWA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kipI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kipI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kwa OCA], [http://pdbe.org/2kwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kwa RCSB], [http://www.ebi.ac.uk/pdbsum/2kwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kwa ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kwa OCA], [https://pdbe.org/2kwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kwa RCSB], [https://www.ebi.ac.uk/pdbsum/2kwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kwa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KIPI_BACSU KIPI_BACSU]] Is a potent inhibitor of the autophosphorylation reaction of kinase A and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. KipI is an inhibitor of the catalytic domain of kinase A affecting the ATP/ADP reactions and not the phosphotransferase functions of this domain. The inhibition is noncompetitive with respect to ATP. | + | [[https://www.uniprot.org/uniprot/KIPI_BACSU KIPI_BACSU]] Is a potent inhibitor of the autophosphorylation reaction of kinase A and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. KipI is an inhibitor of the catalytic domain of kinase A affecting the ATP/ADP reactions and not the phosphotransferase functions of this domain. The inhibition is noncompetitive with respect to ATP. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacsu]] | | [[Category: Bacsu]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Hynson, R M.G]] | | [[Category: Hynson, R M.G]] |
| | [[Category: Jacques, D A]] | | [[Category: Jacques, D A]] |
| Structural highlights
Function
[KIPI_BACSU] Is a potent inhibitor of the autophosphorylation reaction of kinase A and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. KipI is an inhibitor of the catalytic domain of kinase A affecting the ATP/ADP reactions and not the phosphotransferase functions of this domain. The inhibition is noncompetitive with respect to ATP.
Publication Abstract from PubMed
In Bacillus subtilis, the KipI protein is a regulator of the phosphorelay governing the onset of sporulation. KipI binds the relevant sensor histidine kinase, KinA, and inhibits the autophosphorylation reaction. Gene homologues of kipI are found almost ubiquitously throughout the bacterial kingdom and are usually located adjacent to, and often fused with, kipA gene homologues. In B. subtilis, the KipA protein inhibits the antikinase activity of KipI thereby permitting sporulation. We have used a combination of biophysical techniques in order to understand the domain structure and shape of the KipI-KipA complex and probe the nature of the interaction. We also have solved the crystal structure of TTHA0988, a Thermus thermophilus protein of unknown function that is homologous to a KipI-KipA fusion. This structure, which is the first to be described for this class of proteins, provides unique insight into the nature of the KipI-KipA complex. The structure confirms that KipI and KipA are proteins with two domains, and the C-terminal domains belong to the cyclophilin family. These cyclophilin domains are positioned in the complex such that their conserved surfaces face each other to form a large "bicyclophilin" cleft. We discuss the sequence conservation and possible roles across species of this near-ubiquitous protein family, which is poorly understood in terms of function.
A Novel Structure of an Antikinase and its Inhibitor.,Jacques DA, Langley DB, Hynson RM, Whitten AE, Kwan A, Guss JM, Trewhella J J Mol Biol. 2010 Nov 2. PMID:21050859[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jacques DA, Langley DB, Hynson RM, Whitten AE, Kwan A, Guss JM, Trewhella J. A Novel Structure of an Antikinase and its Inhibitor. J Mol Biol. 2010 Nov 2. PMID:21050859 doi:10.1016/j.jmb.2010.10.047
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