2kwa

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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 subtilis1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis

Structural highlights

2kwa is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2]

References

  1. Niehaus TD, Elbadawi-Sidhu M, de Crecy-Lagard V, Fiehn O, Hanson AD. Discovery of a widespread prokaryotic 5-oxoprolinase that was hiding in plain sight. J Biol Chem. 2017 Sep 29;292(39):16360-16367. doi: 10.1074/jbc.M117.805028. Epub , 2017 Aug 22. PMID:28830929 doi:http://dx.doi.org/10.1074/jbc.M117.805028
  2. Wang L, Grau R, Perego M, Hoch JA. A novel histidine kinase inhibitor regulating development in Bacillus subtilis. Genes Dev. 1997 Oct 1;11(19):2569-79. doi: 10.1101/gad.11.19.2569. PMID:9334321 doi:http://dx.doi.org/10.1101/gad.11.19.2569
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OCA