5NOD

PASTA subunit 4 of Streptococcus pneumoniae STKP crystallized with PEG and succinate

Summary for 5NOD

• Entry DOI: 10.2210/pdb5nod/pdb
• Descriptor: Serine/threonine-protein kinase StkP (2 entities in total)
• Functional Keywords: pasta, extracellular domain, ser/thr kinase, streptococcus pneumoniae, transferase
• Biological source: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
• Total number of polymer chains: 1
• Total formula weight: 9084.47

Authors

Galisson, F.,Gueguen-Chaignon, V.,Gouet, P.,Grangeasse, C.,Zucchini, L. (deposition date: 2017-04-12, release date: 2017-11-08, Last modification date: 2024-01-17)

Primary citation

Zucchini, L.,Mercy, C.,Garcia, P.S.,Cluzel, C.,Gueguen-Chaignon, V.,Galisson, F.,Freton, C.,Guiral, S.,Brochier-Armanet, C.,Gouet, P.,Grangeasse, C.
PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae.
Nat Microbiol, 3:197-209, 2018

PubMed Abstract: Eukaryotic-like serine/threonine kinases (eSTKs) with extracellular PASTA repeats are key membrane regulators of bacterial cell division. How PASTA repeats govern eSTK activation and function remains elusive. Using evolution- and structural-guided approaches combined with cell imaging, we disentangle the role of each PASTA repeat of the eSTK StkP from Streptococcus pneumoniae. While the three membrane-proximal PASTA repeats behave as interchangeable modules required for the activation of StkP independently of cell wall binding, they also control the septal cell wall thickness. In contrast, the fourth and membrane-distal PASTA repeat directs StkP localization at the division septum and encompasses a specific motif that is critical for final cell separation through interaction with the cell wall hydrolase LytB. We propose a model in which the extracellular four-PASTA domain of StkP plays a dual function in interconnecting the phosphorylation of StkP endogenous targets along with septal cell wall remodelling to allow cell division of the pneumococcus.

PubMed: 29203882
DOI: 10.1038/s41564-017-0069-3

Experimental method

X-RAY DIFFRACTION (1.9 Å)