5JD9

Bacillus cereus CotH kinase

Summary for 5JD9

• Entry DOI: 10.2210/pdb5jd9/pdb
• Related: 5JD9
• Descriptor: Spore coat protein H, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: atypical kinase fold, structural protein
• Biological source: Bacillus cereus (strain ATCC 10987 / NRS 248)
• Total number of polymer chains: 1
• Total formula weight: 42888.61

Authors

Tomchick, D.R.,Tagliabracci, V.S.,Sreelatha, A. (deposition date: 2016-04-15, release date: 2016-05-18, Last modification date: 2024-03-06)

Primary citation

Nguyen, K.B.,Sreelatha, A.,Durrant, E.S.,Lopez-Garrido, J.,Muszewska, A.,Dudkiewicz, M.,Grynberg, M.,Yee, S.,Pogliano, K.,Tomchick, D.R.,Pawowski, K.,Dixon, J.E.,Tagliabracci, V.S.
Phosphorylation of spore coat proteins by a family of atypical protein kinases.
Proc.Natl.Acad.Sci.USA, 113:E3482-E3491, 2016

PubMed Abstract: The modification of proteins by phosphorylation occurs in all life forms and is catalyzed by a large superfamily of enzymes known as protein kinases. We recently discovered a family of secretory pathway kinases that phosphorylate extracellular proteins. One member, family with sequence similarity 20C (Fam20C), is the physiological Golgi casein kinase. While examining distantly related protein sequences, we observed low levels of identity between the spore coat protein H (CotH), and the Fam20C-related secretory pathway kinases. CotH is a component of the spore in many bacterial and eukaryotic species, and is required for efficient germination of spores in Bacillus subtilis; however, the mechanism by which CotH affects germination is unclear. Here, we show that CotH is a protein kinase. The crystal structure of CotH reveals an atypical protein kinase-like fold with a unique mode of ATP binding. Examination of the genes neighboring cotH in B. subtilis led us to identify two spore coat proteins, CotB and CotG, as CotH substrates. Furthermore, we show that CotH-dependent phosphorylation of CotB and CotG is required for the efficient germination of B. subtilis spores. Collectively, our results define a family of atypical protein kinases and reveal an unexpected role for protein phosphorylation in spore biology.

PubMed: 27185916
DOI: 10.1073/pnas.1605917113

Experimental method

X-RAY DIFFRACTION (1.63 Å)