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Sequence-specific backbone ¹H, ¹³C and ¹?N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc.

ABSTRACT: Protein tyrosine kinases in bacteria are structurally and functionally distinct from their eukaryotic counterparts. The largest family of bacterial tyrosine kinases, the BY-kinase family, is highly conserved in Gram-negative and Gram-positive species, and plays a central role in biofilm and capsule formation. In Escherichia coli the BY-kinase, Wzc, is a critical component of the machinery responsible for the synthesis and export of the exo-polysaccharide colanic acid, a key constituent of biofilms. Here we present the main-chain (1)H(N), (15)N, (13)C' and (13)C?, side-chain (13)C? resonance assignments for a construct that encodes the entire 274-residue cytosolic catalytic domain of Wzc.

SUBMITTER: Temel DB

PROVIDER: S-EPMC3626743 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Sequence-specific backbone ¹H, ¹³C and ¹⁵N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc.

Temel Deniz B DB Dutta Kaushik K Ghose Ranajeet R

Biomolecular NMR assignments 20121208 1

Protein tyrosine kinases in bacteria are structurally and functionally distinct from their eukaryotic counterparts. The largest family of bacterial tyrosine kinases, the BY-kinase family, is highly conserved in Gram-negative and Gram-positive species, and plays a central role in biofilm and capsule formation. In Escherichia coli the BY-kinase, Wzc, is a critical component of the machinery responsible for the synthesis and export of the exo-polysaccharide colanic acid, a key constituent of biofil ...[more]

PMID: 23225198

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