2kwa: Difference between revisions
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New page: '''Unreleased structure''' The entry 2kwa is ON HOLD Authors: Hynson, R.M G., Kwan, A.H., Jacques, D.A., Mackay, J.P., Trewhella, J. Description: 1H, 13C and 15N backbone and side chai... |
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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== | |||
<StructureSection load='2kwa' size='340' side='right'caption='[[2kwa]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kwa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PXPB_BACSU PXPB_BACSU] Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (PubMed:28830929). In addition, is a potent inhibitor of the autophosphorylation reaction of kinase A (kinA) and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. 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 non-competitive with respect to ATP (PubMed:9334321).<ref>PMID:28830929</ref> <ref>PMID:9334321</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | |||
[[Category: Large Structures]] | |||
[[Category: Hynson RMG]] | |||
[[Category: Jacques DA]] | |||
[[Category: Kwan A]] | |||
[[Category: Mackay JP]] | |||
[[Category: Trewhella J]] | |||
Latest revision as of 06:49, 1 May 2024
1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis
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