1knx
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HPr kinase/phosphatase from Mycoplasma pneumoniae
OverviewOverview
HPr kinase/phosphatase (HPrK/P) modifies serine 46 of histidine-containing, protein (HPr), the phosphorylation state of which is the control point of, carbon catabolite repression in low G+C Gram-positive bacteria. To, understand the structural mechanism by which HPrK/P carries out its dual, competing activities we determined the structure of full length HPrK/P, from Mycoplasma pneumoniae (PD8 ID, 1KNX) to 2.5A resolution. The enzyme, forms a homo-hexamer with each subunit containing two domains connected by, a short loop. The C-terminal domain contains the well-described P-loop, (Walker A box) ATP binding motif and takes a fold similar to, phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as, recently described in other HPrK/P structures. As expected, the C-terminal, domain is very similar to the C-terminal fragment of Lactobacillus casei, HPrK/P and the C-terminal domain of Staphylococcus xylosus HPrK/P; the, N-terminal domain is very similar to the N-terminal domain of S.xylosus, HPrK/P. Unexpectedly, the N-terminal domain resembles, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase, (MurE), yet the function of this domain is unclear. We discuss these, observations as well as the structural significance of mutations in the, P-loop and HPrK/P family sequence motif.
About this StructureAbout this Structure
1KNX is a Single protein structure of sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae., Allen GS, Steinhauer K, Hillen W, Stulke J, Brennan RG, J Mol Biol. 2003 Feb 28;326(4):1203-17. PMID:12589763
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