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4KQB

crystal structure of the Golgi casein kinase with Mn/ADP bound

Summary for 4KQB
Entry DOI10.2210/pdb4kqb/pdb
Related4KQA
DescriptorProtein H03A11.1, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordssecreted kinase, transferase
Biological sourceCaenorhabditis elegans (nematode)
Total number of polymer chains2
Total formula weight109286.15
Authors
Xiao, J. (deposition date: 2013-05-14, release date: 2013-06-26, Last modification date: 2024-11-20)
Primary citationXiao, J.,Tagliabracci, V.S.,Wen, J.,Kim, S.A.,Dixon, J.E.
Crystal structure of the Golgi casein kinase.
Proc.Natl.Acad.Sci.USA, 110:10574-10579, 2013
Cited by
PubMed Abstract: The family with sequence similarity 20 (Fam20) kinases phosphorylate extracellular substrates and play important roles in biomineralization. Fam20C is the Golgi casein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Mutations in Fam20C cause Raine syndrome, an osteosclerotic bone dysplasia. Here we report the crystal structure of the Fam20C ortholog from Caenorhabditis elegans. The nucleotide-free and Mn/ADP-bound structures unveil an atypical protein kinase-like fold and highlight residues critical for activity. The position of the regulatory αC helix and the lack of an activation loop indicate an architecture primed for efficient catalysis. Furthermore, several distinct elements, including the presence of disulfide bonds, suggest that the Fam20 family diverged early in the evolution of the protein kinase superfamily. Our results reinforce the structural diversity of protein kinases and have important implications for patients with disorders of biomineralization.
PubMed: 23754375
DOI: 10.1073/pnas.1309211110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.045 Å)
Structure validation

227561

건을2024-11-20부터공개중

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