6g4j | pdb_00006g4j

Structure of the protein kinase YabT from Bacillus subtilis in complex with an alphaREP crystallization helper

spinqualitylabelsall models 6g4j, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6g4j is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.599Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PKN1_BACSU Publication Abstract from PubMed YabT is a serine/threonine kinase of the Hanks family from Bacillus subtilis, which lacks the canonical extracellular signal receptor domain but is anchored to the membrane through a C-terminal transmembrane helix. A previous study demonstrated that a basic juxtamembrane region corresponds to a DNA-binding motif essential for the activation of YabT trans-autophosphorylation. YabT is expressed during spore development and localizes to the asymmetric septum where it specifically phosphorylates essential proteins involved in genome maintenance, such as RecA, SsbA, and YabA. YabT has also been shown to phosphorylate proteins involved in protein synthesis, such as AbrB and Ef-Tu, suggesting a possible regulatory role in the progressive metabolic quiescence of the forespore. Finally, cross phosphorylations with other protein kinases implicate YabT in the regulation of numerous other cellular processes. Using an artificial protein scaffold as crystallization helper, we determined the first crystal structure of this DNA-dependent bacterial protein kinase. This allowed us to trap the active conformation of the kinase domain of YabT. Using NMR, we showed that the basic juxtamembrane region of YabT is disordered in the absence of DNA in solution, just like it is in the crystal, and that it is stabilized upon DNA binding. In comparison with its closest structural homolog, the mycobacterial kinase PknB allowed us to discuss the dimerization mode of YabT. Together with phosphorylation assays and DNA-binding experiments, this structural analysis helped us to gain new insights into the regulatory activation mechanism of YabT. Structural Analysis of the Hanks-Type Protein Kinase YabT From Bacillus subtilis Provides New Insights in its DNA-Dependent Activation.,Shi L, Cavagnino A, Rabefiraisana JL, Lazar N, Li de la Sierra-Gallay I, Ochsenbein F, Valerio-Lepiniec M, Urvoas A, Minard P, Mijakovic I, Nessler S Front Microbiol. 2019 Jan 8;9:3014. doi: 10.3389/fmicb.2018.03014. eCollection , 2018. PMID:30671027 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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