9ruk | pdb_00009ruk

Streptococcus pneumoniae StkP catalytic domain T167A/T169A double mutant in complex with AMP-PNP and Mn2+

spinqualitylabelsall models 9ruk, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ruk is a 2 chain structure with sequence from Streptococcus pneumoniae R6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: ANP, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function STKP_STRR6 Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP (shown in the avirulent strain Rx / Cp1015); PhpP and StkP appear to constitute a functional signaling couple in vivo.

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